[ccp4bb] PhD position available AgResearch & Massey University, New Zealand

[Sutherland-Smith, Andrew]

Applications are invited for a Royal Society of New Zealand Marsden Fund PhD 
scholarship at AgResearch and the Institute of Fundamental Sciences, Massey 
University, Palmerston North, New Zealand.

Evolution Of The Archaeal Cell Wall: Structural Biology And Biochemistry Of 
Archaeal Cell Wall Synthetic Enzymes
 
 “The writing is on the wall: Elucidating the deep evolutionary links between 
cell wall synthesis in bacteria and methanogenic archaea”.
 
The project will investigate the early evolution of cell walls in methanogenic 
archaea. Certain methanogenic archaea contain a pseudomurein cell wall, which 
is structurally analogous to bacterial murein (e.g. peptidoglycan), but there 
are important differences in the chemistry between the two polymers. 
Pseudomurein-containing methanogens use only L-amino acids, contain an 
archaeal-specific sugar and use several unusual peptide bonds. Surprisingly, 
genetic and sequence analyses suggests that the two cell wall synthesis 
pathways share a number of distantly-related enzymes and therefore share a deep 
evolutionary history. This PhD project will investigate these deep evolutionary 
connections using thermophilic methanogens as model organisms and will focus on 
the synthesis of the glycan backbone of the methanogen cell walls. A separate 
PhD position in the overall project has been filled will investigate (in 
parallel) the synthesis of the cross-linking peptide.
 
The scholarship is available now, candidates are encouraged to apply (cover 
letter, CV & academic record) as soon as possible (closing date is September 
5th, 2014). Applicants must meet the requirements for entry into the Massey PhD 
program. The candidates will ideally have a strong interest and research 
background in structural biology and biochemistry.  The stipend is $NZ 30,500 
per year for three years and the Massey University fees are also paid from the 
grant.
 
The primary supervisors include Dr Ron Ronimus (AgResearch) and Dr Andrew 
Sutherland-Smith (IFS, Massey University). The Marsden project also includes 
collaboration with Professor William Martin, University of Dusseldorf, Germany.
 
Interested persons can contact principle investigator Dr Ron Ronimus 
(ron.roni...@agresearch.co.nz, phone (+64-6-351-8036) or Fax (+64-6-351-8003). 
Alternatively, interested persons can contact Dr Andrew Sutherland-Smith 
(a.j.sutherland-sm...@massey.ac.nz).

Andrew Sutherland-Smith, PhD
Biochemistry, Biotechnology & Biomedical Science
Institute of Fundamental Sciences
Massey University
Private Bag 11222
Palmerston North 4442
New Zealand

Phone: +6463569099 x84701

Re: [ccp4bb] MrBump doesn't work (6.4.0 update)

[Marjolein Thunnissen]

Hi

I just encountered the same problem as described in the message below. I tried 
to search but couldn’t find an answer, but was a solution for this problem 
found?

Thanks

Marjolein


On 04 Aug 2014, at 03:59, Eze Chivi 
mailto:ezech...@outlook.com.ar>> wrote:

Hello, I have a problem with the update 6.4.0 of ccp4: MrBump does not start, 
it freezes in the message "Please wait...drawing task window mrbump" and the 
error "expected integer but got """. Sometimes, MrBump starts, but drop-down 
menu doesn't work. Same problem in Linux or Windows versions.
Thank you

Ezequiel

[cid:3A2194AC-734C-45EB-B5A7-CE7FC0F0F1BC]




Marjolein Thunnissen
Science Coordinator MX

MAX IV Laboratory
Lund University
P.O. Box 118, SE-221 00 Lund, Sweden
Visiting address: Ole Römers väg 1, 223 63 Lund
Telephone: +46 766 32 04 17
www.maxlab.lu.se

[ccp4bb]

[Ed Pozharski]

Try refining your model both ways (with and without covalent link) and see if 
electron density maps give you an indication.  At this resolution there will be 
some model bias, so be critical. 


Sent on a Sprint Samsung Galaxy S® III

 Original message From: rohit kumar 
 Date:08/19/2014  2:56 AM  (GMT-05:00) 
To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] 
Dear All,
i have solved a structure of 3.2 A. That is a PLP depended enzyme. 
In their resting state, PLP-dependent enzymes are usually joined by a covalent 
aldimine linkage to an essential lysine residue with a C=N bond. This generates 
the so-called internal aldimine moiety.
Could anybody tell me how we can say that this  PLP is covalently attached to 
the Lys or its making Schiff base or not. 

-- 
WITH REGARDS
Rohit Kumar Singh
Lab. no. 430,
P.I. Dr. S. Gourinath,
School of Life Sciences,
Jawaharlal Nehru University
New Delhi -110067

[ccp4bb] 3rd call, CCP4 structure solution workshop at the Photon Factory

[Charles Ballard]

Dear Colleagues,

we are pleased to announce the  CCP4 structure solution school at the Photon 
Factory, Tsukuba. All details can be found at 
http://www.ccp4.ac.uk/schools/Japan-2014

Title:
"CCP4 school: From data processing to structure refinement and beyond"
Dates: November 4 to 8, 2014
Site: The Photon Factory. Tsukuba, Japan

The school content:

Software workshop: The rest of the time after data collection will feature many 
modern crystallographic software packages taught by authors and other experts. 
It will be organized in three Sections - lectures, tutorials and hands-on 
trouble-shooting.
There will be model data sets available for tutorials but data, provided by 
participants, will have higher priority for the hands-on sessions.

Applicants:

Graduate students, postdoctoral researchers and young scientists at the 
assistant professor level are encouraged to apply. Only 20 applicants will be 
selected for participation. Participants of the workshop are strongly 
encouraged to bring their own problem data sets so the problems can be 
addressed during data collection workshop and/or hands-on sessions.

Application:

Application deadline is 13 September. Application form, the program, contact 
info and other details can be found at 
http://www.ccp4.ac.uk/schools/Japan-2014/index.php

Fees: 

There is no fee for the workshop, but the students will be responsible for 
their transportation and accommodation costs.  A limited number of places will 
be available in the KEK dormitory on a first come basis.

Naohiro Matsugaki, Charles Ballard
-- 
Scanned by iCritical.

Re: [ccp4bb] MrBump doesn't work (6.4.0 update)

[Ronan Keegan]

Hi Marjolein,

I'm glad to hear that. You may also be interested in the new CCP4 online 
service which hosts, among other applications, a MrBUMP service. One of 
the main advantages it has is that it uses HHPred to search for MR 
search models which can produce better models than the simple Fasta 
search performed in the older MrBUMP. You can access it here:


www.ccp4.ac.uk/ccp4online

Best wishes,

Ronan

On 19/08/14 12:22, Marjolein Thunnissen wrote:

Hii Ronan,

Hi,

Embarrassingly enough, my problem has disappeared...I guess indeed it 
was the update, as I updated ccp4 today and now I tried and it works!


Thanks!

Marjolein


On 19 Aug 2014, at 12:28, Ronan Keegan > wrote:




Hi Marjolein,

Thanks for your email and sorry to hear about your problems with 
MrBUMP. Can you please tell me what OS you are using (Linux, Mac 
etc.)? Also us your CCP4 installation completely up to date? There 
should 20 updates in total installed. The last one has some important 
fixes for MrBUMP.


Best wishes,

Ronan

On 19/08/14 09:28, Marjolein Thunnissen wrote:

Hi

I just encountered the same problem as described in the message 
below. I tried to search but couldn’t find an answer, but was a 
solution for this problem found?


Thanks

Marjolein


On 04 Aug 2014, at 03:59, Eze Chivi > wrote:


Hello, I have a problem with the update 6.4.0 of ccp4: MrBump does 
not start, it freezes in the message "Please wait...drawing task 
window mrbump" and the error "expected integer but got """. 
Sometimes, MrBump starts, but drop-down menu doesn't work. Same 
problem in Linux or Windows versions.

Thank you

Ezequiel



*



**Marjolein Thunnissen*
Science Coordinator MX

MAX IV Laboratory
Lund University
P.O. Box 118, SE-221 00 Lund, Sweden
Visiting address: Ole Römers väg 1, 223 63 Lund
Telephone: +46 766 32 04 17
www.maxlab.lu.se 




--
Scanned by iCritical.




*



**Marjolein Thunnissen*
Science Coordinator MX

MAX IV Laboratory
Lund University
P.O. Box 118, SE-221 00 Lund, Sweden
Visiting address: Ole Römers väg 1, 223 63 Lund
Telephone: +46 766 32 04 17
www.maxlab.lu.se 




--
Scanned by iCritical.

[ccp4bb] Slightly O-T: Hodgkin vs. Thatcher.

[Ian Tickle]

All, slightly off-topic, but this might be interesting (BBC Radio 4
tomorrow @ 14:15 BST):

http://www.bbc.co.uk/programmes/b04dmxwj

For some background info see also:

http://www.theguardian.com/science/political-science/2014/aug/13/margaret-thatchers-surprising-relationship-with-dorothy-hodgkin

Cheers

-- Ian

Re: [ccp4bb] Removing PEG3350

[Keller, Jacob]

Aren't the many chromatographies out there sufficient? Or ultrafiltration? Can 
you be a bit more specific about your needs?

JPK


-Original Message-
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Reza 
Khayat
Sent: Tuesday, August 19, 2014 9:55 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] Removing PEG3350

Hi,

Does anyone have a protocol for getting rid of PEG3350 from a protein sample? 

Best wishes,
Reza

Reza Khayat, PhD
Assistant Professor
The City College of New York
Department of Chemistry, MR-1135
160 Convent Avenue
New York, NY  10031
Tel. (212) 650-6070
www.khayatlab.org

Re: [ccp4bb] Removing PEG3350

[Remie Fawaz-Touma]

Hi Reza, I had to do this before. 

This protocol works for any PEG and any chemical to be removed from a solution: 
buffer exchange into the new buffer you want your protein to be in. There are 
ways to do that by 15 mL Amicon concentrators from millipore for large volumes, 
or if your protein is already concentrated, there are some small 0.5 mL 
concentrators from millipore as well.

The key is to keep your spinning at low speeds (concentrators manuals will tell 
you) so you don’t precipitate or loose your protein. Check your protein 
concentration every 2 hours just to make sure you are not loosing it on 
concentrator surfaces and so on. 

Good Luck,
Remie

On Aug 19, 2014, at 9:55 AM, Reza Khayat  wrote:

> Hi,
> 
> Does anyone have a protocol for getting rid of PEG3350 from a protein sample? 
> 
> Best wishes,
> Reza
> 
> Reza Khayat, PhD
> Assistant Professor
> The City College of New York
> Department of Chemistry, MR-1135
> 160 Convent Avenue
> New York, NY  10031
> Tel. (212) 650-6070
> www.khayatlab.org

[ccp4bb] Removing PEG3350

[Reza Khayat]

Hi,

Does anyone have a protocol for getting rid of PEG3350 from a protein sample? 

Best wishes,
Reza

Reza Khayat, PhD
Assistant Professor
The City College of New York
Department of Chemistry, MR-1135
160 Convent Avenue
New York, NY  10031
Tel. (212) 650-6070
www.khayatlab.org

Re: [ccp4bb] Enigmatic electron density attached to Cys residue

[Mark J van Raaij]

What odds to you give us?
...I bet on disordered DTT covalently bound to the protein.

Mark J van Raaij
Lab 20B
Dpto de Estructura de Macromoleculas
Centro Nacional de Biotecnologia - CSIC
c/Darwin 3
E-28049 Madrid, Spain
tel. (+34) 91 585 4616
http://www.cnb.csic.es/~mjvanraaij







On 19 Aug 2014, at 16:12, Bernhard Loll wrote:

> Dear all,
>  
> We are currently working on a small GTPase. The structure has been solved to 
> 1.4 A with two molecules in the ASU. In the difference electron density we 
> can clearly see difference density (in one monomer) attached to a Cys residue.
>  
> The protein has been expressed in E. coli. For crystallization experiments 
> the GTPase was incubated with GMPPNP, that had been dissolved in 20 mM HEPES 
> pH 7.5 and 50 mM NaCl. Prior to crystallization
> the protein was stored in a buffer composed of 20 mM HEPES pH 7.5, 200 mM 
> NaCl, 5 mM, Mg acetate, 2 mM DTT and 2% (v/v) glycerol.
>  
> The protein crystallized under the following conditions:
> 28% (v/v) PEG 200, 5% (w/v) PEG 3000 and 100 mM MES buffer at pH 6.0
>  
> The anomalous signal is too weak to judge the positions of the sulphur atoms. 
> We have performed MS analysis on the protein before crystallization and on 
> dissolved protein crystals. MS revealed a mass difference of about 135 Da, 
> indicating that some chemistry must have went on in the crystallization drop.
>  
> The extra electron density has a planar shape and is quite symmetric. We have 
> placed some dummy water molecules in the density. Distances are given in A in 
> the PNG file.
>  
> Attached files
>  
> coot1.png: 2FoFc electron density map (blue) @ sigma=1 and FoFc electron 
> density map (blue) @ sigma=+3 after phenix.refine
> coot2.png: same electron densities as in coot1.png, with dummy atoms placed
> coot3.png: same electron densities as in coot1.png, side view
>  
> Thanks for your time and efforts.
>  
> Cheers,
>  
> Bernhard
> -- 
> Dr. Bernhard Loll
> Freie Universitaet Berlin
> Fachbereich Biologie, Chemie, Pharmazie
> Institut fuer Chemie und Biochemie
> AG Strukturbiochemie
> Takustr. 6
> D-14195 Berlin
> Germany
> 
> Phone: +49 (0) 30 838-57348
> Fax:   +49 (0) 30 838-457348
> Email: 
> l...@chemie.fu-berlin.de
> 
> Homepage: 
> http://www.bcp.fu-berlin.de/chemie/bc/ag/agwahl/
> 

Re: [ccp4bb] Removing PEG3350

[Alexander Aleshin]

Remie,
Actually, concentrating of a protein solution is not the best approach to 
removing low MW impurities, gel filtration chromatography is  more reliable and 
... faster.

Regards,
Alex

On Aug 19, 2014, at 7:03 AM, Remie Fawaz-Touma wrote:

Hi Reza, I had to do this before.

This protocol works for any PEG and any chemical to be removed from a solution: 
buffer exchange into the new buffer you want your protein to be in. There are 
ways to do that by 15 mL Amicon concentrators from millipore for large volumes, 
or if your protein is already concentrated, there are some small 0.5 mL 
concentrators from millipore as well.

The key is to keep your spinning at low speeds (concentrators manuals will tell 
you) so you don’t precipitate or loose your protein. Check your protein 
concentration every 2 hours just to make sure you are not loosing it on 
concentrator surfaces and so on.

Good Luck,
Remie

On Aug 19, 2014, at 9:55 AM, Reza Khayat 
mailto:rkha...@ccny.cuny.edu>> wrote:

Hi,

Does anyone have a protocol for getting rid of PEG3350 from a protein sample?

Best wishes,
Reza

Reza Khayat, PhD
Assistant Professor
The City College of New York
Department of Chemistry, MR-1135
160 Convent Avenue
New York, NY  10031
Tel. (212) 650-6070
www.khayatlab.org

Re: [ccp4bb] Enigmatic electron density attached to Cys residue

[Reza Khayat]

Hi,

I guessed glycerol by looking at the figs and not reading your text. Having 
read your text afterwards, you do have glycerol in the solution. My guess is 
glycerol.
 
Best wishes,
Reza

Reza Khayat, PhD
Assistant Professor
The City College of New York
Department of Chemistry, MR-1135
160 Convent Avenue
New York, NY  10031
Tel. (212) 650-6070
www.khayatlab.org


 Original message 
>Date: Tue, 19 Aug 2014 16:39:36 +0200
>From: CCP4 bulletin board  (on behalf of Mark J van 
>Raaij )
>Subject: Re: [ccp4bb] Enigmatic electron density attached to Cys residue  
>To: CCP4BB@JISCMAIL.AC.UK
>
>What odds to you give us?
>...I bet on disordered DTT covalently bound to the protein.
>
>Mark J van Raaij
>Lab 20B
>Dpto de Estructura de Macromoleculas
>Centro Nacional de Biotecnologia - CSIC
>c/Darwin 3
>E-28049 Madrid, Spain
>tel. (+34) 91 585 4616
>http://www.cnb.csic.es/~mjvanraaij
>
>
>
>
>
>
>
>On 19 Aug 2014, at 16:12, Bernhard Loll wrote:
>
>> Dear all,
>>  
>> We are currently working on a small GTPase. The structure has been solved to 
>> 1.4 A with two molecules in the ASU. In the difference electron density we 
>> can clearly see difference density (in one monomer) attached to a Cys 
>> residue.
>>  
>> The protein has been expressed in E. coli. For crystallization experiments 
>> the GTPase was incubated with GMPPNP, that had been dissolved in 20 mM HEPES 
>> pH 7.5 and 50 mM NaCl. Prior to crystallization
>> the protein was stored in a buffer composed of 20 mM HEPES pH 7.5, 200 mM 
>> NaCl, 5 mM, Mg acetate, 2 mM DTT and 2% (v/v) glycerol.
>>  
>> The protein crystallized under the following conditions:
>> 28% (v/v) PEG 200, 5% (w/v) PEG 3000 and 100 mM MES buffer at pH 6.0
>>  
>> The anomalous signal is too weak to judge the positions of the sulphur 
>> atoms. We have performed MS analysis on the protein before crystallization 
>> and on dissolved protein crystals. MS revealed a mass difference of about 
>> 135 Da, indicating that some chemistry must have went on in the 
>> crystallization drop.
>>  
>> The extra electron density has a planar shape and is quite symmetric. We 
>> have placed some dummy water molecules in the density. Distances are given 
>> in A in the PNG file.
>>  
>> Attached files
>>  
>> coot1.png: 2FoFc electron density map (blue) @ sigma=1 and FoFc electron 
>> density map (blue) @ sigma=+3 after phenix.refine
>> coot2.png: same electron densities as in coot1.png, with dummy atoms placed
>> coot3.png: same electron densities as in coot1.png, side view
>>  
>> Thanks for your time and efforts.
>>  
>> Cheers,
>>  
>> Bernhard
>> -- 
>> Dr. Bernhard Loll
>> Freie Universitaet Berlin
>> Fachbereich Biologie, Chemie, Pharmazie
>> Institut fuer Chemie und Biochemie
>> AG Strukturbiochemie
>> Takustr. 6
>> D-14195 Berlin
>> Germany
>> 
>> Phone: +49 (0) 30 838-57348
>> Fax:   +49 (0) 30 838-457348
>> Email: 
>> l...@chemie.fu-berlin.de
>> 
>> Homepage: 
>> http://www.bcp.fu-berlin.de/chemie/bc/ag/agwahl/
>> 

Re: [ccp4bb] Removing PEG3350

[R. M. Garavito]

Reza,

If your protein is not too small (>20 kDa), use a spin-column (i.e., desalting 
column) with G-25 sephedex.  It is CHEAP, fast, and the recovery is good.  We 
have even used them to adjust buffer concentrations or to remove micellar 
detergents; we have used protein concentrations up to 10 mg/mL, prior to 
crystallization. 

You will need a clinical centrifuge, G-25 Sephedex (reusable) equilibrated in 
your desired buffer, glass wool, 15 mL plastic conical centrifuge tube 
(reusable), 5 mL syringe barrel (reusable).  

Load the Sephedex into the 5 mL syringe barrel to make a gel bed ≥ 5x the 
sample volume
Put into the 15 mL plastic conical centrifuge tube and spin for 2 min to remove 
excess buffer
Remove the excess buffer from conical centrifuge tube
Add your sample (0.2 mL to 1 mL) to the gel bed, then spin for 2 min to collect 
your cleaned sample.
The sample will be slightly diluted by 10-20% depending on conditions.

We have our students in our undergraduate biochem class do this all the time to 
remove ammonium sulfate from protein samples for assay.  If they can do it.

Or you can buy premade stuff to do the same thing.

Good luck,

Michael


R. Michael Garavito, Ph.D.
Professor of Biochemistry & Molecular Biology
603 Wilson Rd., Rm. 513   
Michigan State University  
East Lansing, MI 48824-1319
Office:  (517) 355-9724 Lab:  (517) 353-9125
FAX:  (517) 353-9334Email:  rmgarav...@gmail.com





On Aug 19, 2014, at 9:55 AM, Reza Khayat  wrote:

> Hi,
> 
> Does anyone have a protocol for getting rid of PEG3350 from a protein sample? 
> 
> Best wishes,
> Reza
> 
> Reza Khayat, PhD
> Assistant Professor
> The City College of New York
> Department of Chemistry, MR-1135
> 160 Convent Avenue
> New York, NY  10031
> Tel. (212) 650-6070
> www.khayatlab.org

Re: [ccp4bb] Enigmatic electron density attached to Cys residue

[Partha]

Hi Bernhard,

It is difficult guess with two dimensional images. Is it possible a metal 
coordinated by Cys-Sulfur and one or two acetate ions?

HTH,
Partha

Sent from my iPhone

> On Aug 19, 2014, at 10:12 AM, Bernhard Loll  wrote:
> 
> Dear all,
>  
> We are currently working on a small GTPase. The structure has been solved to 
> 1.4 A with two molecules in the ASU. In the difference electron density we 
> can clearly see difference density (in one monomer) attached to a Cys residue.
>  
> The protein has been expressed in E. coli. For crystallization experiments 
> the GTPase was incubated with GMPPNP, that had been dissolved in 20 mM HEPES 
> pH 7.5 and 50 mM NaCl. Prior to crystallization
> the protein was stored in a buffer composed of 20 mM HEPES pH 7.5, 200 mM 
> NaCl, 5 mM, Mg acetate, 2 mM DTT and 2% (v/v) glycerol.
>  
> The protein crystallized under the following conditions:
> 28% (v/v) PEG 200, 5% (w/v) PEG 3000 and 100 mM MES buffer at pH 6.0
>  
> The anomalous signal is too weak to judge the positions of the sulphur atoms. 
> We have performed MS analysis on the protein before crystallization and on 
> dissolved protein crystals. MS revealed a mass difference of about 135 Da, 
> indicating that some chemistry must have went on in the crystallization drop.
>  
> The extra electron density has a planar shape and is quite symmetric. We have 
> placed some dummy water molecules in the density. Distances are given in A in 
> the PNG file.
>  
> Attached files
>  
> coot1.png: 2FoFc electron density map (blue) @ sigma=1 and FoFc electron 
> density map (blue) @ sigma=+3 after phenix.refine
> coot2.png: same electron densities as in coot1.png, with dummy atoms placed
> coot3.png: same electron densities as in coot1.png, side view
>  
> Thanks for your time and efforts.
>  
> Cheers,
>  
> Bernhard
> -- 
> Dr. Bernhard Loll
> Freie Universitaet Berlin
> Fachbereich Biologie, Chemie, Pharmazie
> Institut fuer Chemie und Biochemie
> AG Strukturbiochemie
> Takustr. 6
> D-14195 Berlin
> Germany
> 
> Phone: +49 (0) 30 838-57348
> Fax:   +49 (0) 30 838-457348
> Email: l...@chemie.fu-berlin.de
> Homepage: http://www.bcp.fu-berlin.de/chemie/bc/ag/agwahl/
> 
> 
> 

[ccp4bb] ccp4 QTMG

[PC]

Hi,I used COOT mask map by atom selection and cut out a fragment of the map, then exported it and now I tried to open it in QTMG.It displays it as a unit cell,  I want one for a presentation, how can I combine it to display one image ?Thank you,Patrick


Free 3D Earth Screensaver
Watch the Earth right on your desktop! Check it out at www.inbox.com/earth

Re: [ccp4bb] ccp4 QTMG

[Jon Agirre]

You can create the same selection in CCP4mg, display the map and then,
clicking on the first icon on the left underneath the map's name, use Clip
and choose your atom selection. Then, in Clip Radius you can adjust how
much of the map you want to see.

Hope this helps,
Jon


On 19 August 2014 12:06, PC  wrote:

>  Hi,
>
> I used COOT mask map by atom selection and cut out a fragment of the map,
> then exported it and now I tried to open it in QTMG.
>
> It displays it as a unit cell,  I want one for a presentation, how can I
> combine it to display one image ?
>
> Thank you,
> Patrick
> --
>  [image: 3D Earth Screensaver Preview] 
> *Free 3D Earth Screensaver*
> Watch the Earth right on your desktop! Check it out at www.inbox.com/earth
>



-- 
Dr Jon Agirre
York Structural Biology Laboratory / Department of Chemistry
University of York, Heslington, YO10 5DD, York, England
http://www.york.ac.uk/chemistry/research/ysbl/people/research/jagirre/
+44 (0) 1904 32 8253

[ccp4bb] Postdoctoral positions at Monash University

[Dominika Elmlund]

Dear Crystallographers:

We are starting a new electron microscopy/biochemistry laboratory at Monash
University, Melbourne, Australia (http://www.monash.edu.au/). Monash is a
young university (founded 1958) that has already made it to the top one per
cent of the world's universities according to the Times Higher Education
World University Rankings.

We have two postdoctoral positions available. One could be suitable for an
individual with extensive experience in theory/algorithm development for
crystallographic data processing and the other could be suitable for a
crystallographer with a strong biochemical background that wants to branch
into the field of cryo-EM of large macromolecular assemblies.

Our laboratory focuses on two fundamental research directions:
computational method development for single-particle 3D reconstruction at
near-atomic resolution and yeast transcription initiation on TATA-less
promoters.

To find out more about the positions and our research, please visit
http://simple.stanford.edu/emjobs_monash.html. Successful applicants must
have published at least two first-author papers. Interested candidates send
their CV:s and contact info to emjob.mon...@gmail.com.

We would appreciate if you could share this announcement with suitably
skilled and interested scientists in your network.

Best,

Dominika Elmlund & Hans Elmlund


-- 


Dominika Elmlund, PhD
Associate Professor
Dept. Biochemistry and Molecular Biology
School of Biomedical Sciences
Monash University
Bldg. 77, Clayton Vic,
Australia 3800

[ccp4bb] 72nd Pittsburgh Diffraction Conference

[John Rose]

Join us for the seventy second annual Pittsburgh Diffraction Conference  
Ocrober 26th - 28th, 2014.  For more details please visit our website at 
pdc14.bmb.uga.edu  to register by October 15th.



2nd Announcement
The 72nd Annual Pittsburgh Diffraction Conference

October 26 - 28, 2014

Georgia Center for Continuing Education

Athens, GA,

Organized by John Rose and B.C. Wang

 



 

Scientific Sessions
Oct 27 AM Session: 100 years of X-ray Diffraction
 Chair John Rose, University of Georgia
 Brian Matthews (University of Oregon)
 Bi-Cheng Wang (University of Georgia)
 Charles Campana (Bruker-AXS)
 Aina Cohen (Stanford Synchrotron Radiation Laboratory)
 Larry DeLucas (University of Alabama, Birmingham)
 TBA
Oct 27 PM Session: Structure Elucidation, Refinement and Interpretation through 
Powder Diffraction Crystallography

 Chair Charles Lake, Indiana University of Pennsylvania
 Brian Toby (APS, Argonne National Laboratory)
 Bob von Dreele (APS, Argonne National Laboratory)
 Ashfia Huq (SNS, Oak Ridge National Laboratory)
 Angus Wilkinson (Georgia Institute of Technology)
 Clarina dela Cruz (Oak Ridge National Laboratory)
 Scott Spearman (PANanalytical)
 
Oct 28 AM Session: Crystallographic Education

 Chair Joe Ng (University of Alabama, Huntsville)

 Cora Lind-Kovacs (University of Toledo)
 Joe NG (University of Alabama, Huntsville)
 Leighton Coates (Oak Ridge National Laboratory)
 Larry DeLucas (University of Alabama, Birmingham)
 Bill Duax (Hauptman-Woodward Institute)
 Claudia Rawn (University of Tennessee) 
 Oct 28 PM Session: Advances in Neutron Crystallography

 Chair Paul Langan (Oak Ridge National Laboratory)
 Irene Weber (Georgia State University)
 Don Ronning (University of Toledo)
 Andrey Kovalevsky (Oak Ridge National Laboratory)
 TBA
 TBA

 



 

Conference Workshop

Sunday October 26

9:00 - 5:00

Georgia Center for Continuing Education

 

Powder Diffraction Structure Solution with GSAS-II

Robert B. Von Dreele and Brian Toby

X-ray Science Division, Advanced Photon Source, Argonne National Laboratory

 

The new GSAS-II package is believed to be the only general-purpose 
crystallographic analysis package to be started in the current century. It is 
also the only package written in a modern scientist-friendly language, such as 
Python. GSAS-II performs structural analysis from x-ray and neutron diffraction 
data, which may be single-crystal and/or powder diffraction data. It is hoped 
that by the time of the PDC, work will have begun on extending GSAS-II to 
include TOF data from the neutron spallation source.  Beyond structural 
analysis, GSAS-II can be used for powder diffraction data reduction, texture 
and stress analysis as well as pattern indexing and structure solution. 

 

This workshop will highlight these latter capabilities of GSAS-II: indexing and 
structure solution from powder diffraction, although all features of the 
package will be introduced. Participants should bring a laptop (Windows, Mac or 
Linux) with the GSAS-II software installed. To download GSAS-II see 
subversion.xray.aps.anl.gov/trac/pyGSAS.

 

Contact the authors in advance for help with software installation. Limited 
assistance will also be available before the workshop start time.

 

Workshop Registration $65.00 (includes lunch)

Space is limited to 30 participants so register soon!

 

+

 

Deadlines

 

Conference Registrations – Deadline October 15, 2014

Everyone must register for the meeting including invited speakers.

$150 Conference registration for professionals (non students)

$ 50 Conference registration for students

$ 65 GSAS-II Workshop registration

Reservations can be made via the conference web page

pdc14.bmb.uga.edu (REGISTRATIONS)

 

Hotel reservations – Deadline September 29, 2014

The PDS has reserved a block of 40 rooms at the UGA Hotel & Conference Center 
at the conference rate of $104.00 per night.

Hotel reservations may be made via HOUSING link on the PDC web page or by 
telephone (800-884-1381). Please reference the hotel block code 83280 when 
making your reservations.

Abstracts – Deadline September 29, 2014 (See the ABSTRACTS link on the PDC web 
page).

Sidhu Award – Deadline September 15, 2014 (See the SIDHU AWARD link on the PDC 
web page).




For more information please see the PDC Web Site: PDC14.bmb.uga.edu

 

 

John Rose Ph.D.
Associate Professor
B204B, The Fred C. Davison Life Sciences Complex
120 Green Street
Department of Biochemistry and Molecular 

Re: [ccp4bb] Removing PEG3350

[Remie]

Hi Alex, 
I disagree with you even though GF is always the last step in my purifications. 
Because it involves concentration before and after the GF so during the 
concentration you can already be doing the buffer exchange.
You use GF when you want to purify other protein impurities if they are 
different sizes. Of course it has other uses too. But not quite practical for 
just changing buffer also considering the amount of protein you could be 
loosing along the process. If one is careful, centripreps are best for 
concentrating and changing the buffer. I tell you this from experience with 
large hard to express proteins.

Best of luck,
Remie

> On Aug 19, 2014, at 10:45 AM, Alexander Aleshin  
> wrote:
> 
> Remie,
> Actually, concentrating of a protein solution is not the best approach to 
> removing low MW impurities, gel filtration chromatography is  more reliable 
> and ... faster.
> 
> Regards,
> Alex
> 
>> On Aug 19, 2014, at 7:03 AM, Remie Fawaz-Touma wrote:
>> 
>> Hi Reza, I had to do this before. 
>> 
>> This protocol works for any PEG and any chemical to be removed from a 
>> solution: buffer exchange into the new buffer you want your protein to be 
>> in. There are ways to do that by 15 mL Amicon concentrators from millipore 
>> for large volumes, or if your protein is already concentrated, there are 
>> some small 0.5 mL concentrators from millipore as well.
>> 
>> The key is to keep your spinning at low speeds (concentrators manuals will 
>> tell you) so you don’t precipitate or loose your protein. Check your protein 
>> concentration every 2 hours just to make sure you are not loosing it on 
>> concentrator surfaces and so on. 
>> 
>> Good Luck,
>> Remie
>> 
>>> On Aug 19, 2014, at 9:55 AM, Reza Khayat  wrote:
>>> 
>>> Hi,
>>> 
>>> Does anyone have a protocol for getting rid of PEG3350 from a protein 
>>> sample? 
>>> 
>>> Best wishes,
>>> Reza
>>> 
>>> Reza Khayat, PhD
>>> Assistant Professor
>>> The City College of New York
>>> Department of Chemistry, MR-1135
>>> 160 Convent Avenue
>>> New York, NY  10031
>>> Tel. (212) 650-6070
>>> www.khayatlab.org
> 

[ccp4bb]

[Shane Caldwell]

Hi Rohit,

Mass spectrometry might give you the most definitive answer, if you can
denature  or digest and identify the adduct.

In addition, PLP has a characteristic absorbance that can change based on
its chemistry, and so you may be able to probe it spectrophotometrically,
although this might not be as straightforward as MS

Cheers,

Shane Caldwell
McGill University


On Tue, Aug 19, 2014 at 2:56 AM, rohit kumar  wrote:

> Dear All,
> i have solved a structure of 3.2 A. That is a PLP depended enzyme.
> In their resting state, PLP-dependent enzymes are usually joined by a
> covalent aldimine linkage to an essential lysine residue with a C=N bond.
> This generates the so-called internal aldimine moiety.
> Could anybody tell me how we can say that this  PLP is covalently attached
> to the Lys or its making Schiff base or not.
>
> --
> WITH REGARDS
> Rohit Kumar Singh
> Lab. no. 430,
> P.I. Dr. S. Gourinath,
> School of Life Sciences,
> Jawaharlal Nehru University
> New Delhi -110067
>

Re: [ccp4bb] A bug in aimless in last update

[Phil Evans]

There was indeed a bug for which I apologise. It is fixed in version 0.3.11 
which will be filtering through CCP4 updates in due course. In the mean time if 
you get this bug you will have to revert to an earlier version (0.3.6 or 
earlier I think), or you can get it (Linux version) from 

ftp://ftp.mrc-lmb.cam.ac.uk/pub/pre/aimless-0.3.11.linux64

Apologies
Phil


On 12 Aug 2014, at 08:10, Robert Gustafsson  wrote:

> Dear all,
> 
> It seems that the last update of the ccp4 suite contains at least one bug in 
> aimless. Failed every time with the same error message (below) and worked 
> again when update was uninstalled. It is the update 6.4.0-020 that was the 
> cause. 
> 
> Did not know who to send to but hopefully at least someone here knows or is 
> that person.
> 
> Have a nice day!
> 
> Sincerely,
> Robert Gustafsson
> 
> ***
> The program run with command: 
> 
> (Here was a list of files and options such as HKLIN)
> 
> has failed with error message
> Assertion failed: (sd > 0.0), function Average, file 
> /Users/buildbot/Buildslaves/ccp4-slave/release-6_4_0-mac10_6/build/devtools/checkout/aimless/selectedobservations.cpp,
>  line 250.
> ***
> 
> ___
> Robert Gustafsson
> PhD Student
> Department of Biochemistry and Biophysics
> Stockholm University
> 106 91 Stockholm, Sweden
> 
> e-mail: robert.gustafs...@dbb.su.se
> 

[ccp4bb]

[Prashant Deshmukh]

Hi,
i am concentrating my protein using centricon filter, but it is
precipitated soon. Please help me solving this problem.
Thanks.
Prashant Deshmukh
Dept. of Biophysics,
NIMHANS,
Bangalore 560 029,
E-mail:prashantbiophys...@gmail.com
Mob.No.: +919620986525

[ccp4bb]

[Remie Fawaz-Touma]

Hi Prashant,

You need to go really slow when concentrating, not more than 2000 rpm for 
proteins that precipitate easily. Your protein could be sticking to the sides 
of your centricon or precipitating. Follow the manual in getting your protein 
out of the filter (I believe you invert the filter into a clean centricon and 
spin down fast).

If you see the protein precipitating (you see the white chunks), you’ve been 
going too fast. Spin your protein down in a conical tube to get the 
precipitation at the bottom, decant supernatant and check the concentration of 
this supernatant to see if further concentration on this sample is worthwhile.

If not, start with a fresh sample.
Good luck,

Remie

On Aug 19, 2014, at 1:42 PM, Prashant Deshmukh  
wrote:

> Hi,
> i am concentrating my protein using centricon filter, but it is precipitated 
> soon. Please help me solving this problem.
> Thanks. 
> Prashant Deshmukh
> Dept. of Biophysics,
> NIMHANS,
> Bangalore 560 029,
> E-mail:prashantbiophys...@gmail.com
> Mob.No.: +919620986525

[ccp4bb]

[Chris Fage]

Hi Prashant,

I typically stop the centrifuge once in awhile and pipet up/down to prevent
the sample from over-concentrating. Depending on how sensitive the sample
is, you may want to do this once every 10-60 min.

Hope this helps,
Chris


On Tue, Aug 19, 2014 at 1:42 PM, Prashant Deshmukh <
prashantbiophys...@gmail.com> wrote:

> Hi,
> i am concentrating my protein using centricon filter, but it is
> precipitated soon. Please help me solving this problem.
> Thanks.
> Prashant Deshmukh
> Dept. of Biophysics,
> NIMHANS,
> Bangalore 560 029,
> E-mail:prashantbiophys...@gmail.com
> Mob.No.: +919620986525
>

[ccp4bb] Contract Scientist Opening at Sanofi, MA, US

[Ronnie]

Contract
Research Scientist-Principle Research Associate
 
 

 
Job Category   Sanofi/Genzyme - Scientific, Framingham, MA
 
Job Title   Principle Research Associate 
 
 
 
Duties


 
Responsibilities
A highly
motivated candidate is sought to join a state of the art crystallography group
within the Protein Engineering Department at Sanofi Biotherapeutics. The
individual will carry out purification, crystallization of protein targets, and
possibly determining structures of protein-ligands.  A successful
candidate will participate in experimental design and perform complex
analytical procedures with a high degree of independence.
Skills


 
.
Capable of
designing experiments, generating data and interpreting results independently.
Familiarity with lab robotics and automation and other protein biophysical
characterization is preferred.  Strong, concise, and consistent written
and oral communication is required.  Expertise in data collection and
determination with common crystallographic software such as CCP4, HKL, Phenix
is a plus.
Education


 
B.S/M.S in
biochemistry with 8+ years of experience in protein expression, purification,
crystallization with strong protein chemistry skills or a recent Ph.D in
protein crystallography with <1 year of experience post degree.  
Please send CV to ronnie@genzyme.com

[ccp4bb]

[R. M. Garavito]

Prishant,

Remember that concentrating by almost any method is a non-uniform process.  In 
your case, right at the membrane the concentration is much higher than in the 
surrounding solution.  As Chris says, frequent efforts to keep the solution 
well mixed can prevent precipitation.  As you mix, look through the tube 
towards a light to see if you see schlieren patterns, indicative your protein 
concentrating at the membrane.   In the best case, the protein concentration 
may shoot up too high at the membrane, which induces precipitation, and mixing 
more will help. 

In the really worst case scenario, your protein may not be very soluble under 
the conditions you have chosen (i.e., pH, salt, ionic strength).  If so, you 
may need to rethink buffer conditions for concentrating in this manner (E.g., 
more salt, different buffer pH, chaotropic salts like LiCl, etc.).  

Good luck and don't despair yet.  This happens quite often sometimes.

Michael


R. Michael Garavito, Ph.D.
Professor of Biochemistry & Molecular Biology
603 Wilson Rd., Rm. 513   
Michigan State University  
East Lansing, MI 48824-1319
Office:  (517) 355-9724 Lab:  (517) 353-9125
FAX:  (517) 353-9334Email:  rmgarav...@gmail.com





On Aug 19, 2014, at 3:55 PM, Chris Fage  wrote:

> Hi Prashant,
> 
> I typically stop the centrifuge once in awhile and pipet up/down to prevent 
> the sample from over-concentrating. Depending on how sensitive the sample is, 
> you may want to do this once every 10-60 min.
> 
> Hope this helps,
> Chris
> 
> 
> On Tue, Aug 19, 2014 at 1:42 PM, Prashant Deshmukh 
>  wrote:
> Hi,
> i am concentrating my protein using centricon filter, but it is precipitated 
> soon. Please help me solving this problem.
> Thanks. 
> Prashant Deshmukh
> Dept. of Biophysics,
> NIMHANS,
> Bangalore 560 029,
> E-mail:prashantbiophys...@gmail.com
> Mob.No.: +919620986525
> 

Re: [ccp4bb] Enigmatic electron density attached to Cys residue

[Roger Rowlett]

The planarity and symmetry rules out a mixed disulfide with DTT. Wrong
size/shape for glycerol. Without looking at your crystallization reagents,
I would have suggested something like an S-hydroxycysteine adduct of
something like 2,4-pentanedione or a dehydrated MPD alkene. Could
pentanedione be a degradation product of PEG200? Did any MPD get into the
mix? We have seen spurious oxidation of Cys to Cys-OH in thiol proteins,
e,g, PDB 3UAO.

Good luck. With that high quality ED, you'd think it would be easy to ID...

Roger Rowlett

Dear all,



We are currently working on a small GTPase. The structure has been solved
to 1.4 A with two molecules in the ASU. In the difference electron density
we can clearly see difference density (in one monomer) attached to a Cys
residue.



The protein has been expressed in E. coli. For crystallization experiments
the GTPase was incubated with GMPPNP, that had been dissolved in 20 mM
HEPES pH 7.5 and 50 mM NaCl. Prior to crystallization

the protein was stored in a buffer composed of 20 mM HEPES pH 7.5, 200 mM
NaCl, 5 mM, Mg acetate, 2 mM DTT and 2% (v/v) glycerol.



The protein crystallized under the following conditions:

28% (v/v) PEG 200, 5% (w/v) PEG 3000 and 100 mM MES buffer at pH 6.0



The anomalous signal is too weak to judge the positions of the sulphur
atoms. We have performed MS analysis on the protein before crystallization
and on dissolved protein crystals. MS revealed a mass difference of about
135 Da, indicating that some chemistry must have went on in the
crystallization drop.



The extra electron density has a planar shape and is quite symmetric. We
have placed some dummy water molecules in the density. Distances are given
in A in the PNG file.



Attached files



coot1.png: 2FoFc electron density map (blue) @ sigma=1 and FoFc electron
density map (blue) @ sigma=+3 after phenix.refine

coot2.png: same electron densities as in coot1.png, with dummy atoms placed

coot3.png: same electron densities as in coot1.png, side view



Thanks for your time and efforts.



Cheers,



Bernhard

-- 
Dr. Bernhard Loll
Freie Universitaet Berlin
Fachbereich Biologie, Chemie, Pharmazie
Institut fuer Chemie und Biochemie
AG Strukturbiochemie
Takustr. 6
D-14195 Berlin
Germany

Phone: +49 (0) 30 838-57348
Fax:   +49 (0) 30 838-457348
Email: l...@chemie.fu-berlin.de
Homepage: http://www.bcp.fu-berlin.de/chemie/bc/ag/agwahl/

[ccp4bb]

[Roger Rowlett]

Some things to try to increase solubility:

1. Move the buffer pH away from the expected pI. Proteins have minimum
solubility near their pI values.
2. Add solubilizing agents to the solution, e.g., 20-50% glycerol. (This
may alter you crystallization screening strategy)
3. Include some inert salt in the solution to minimize electrostatic
interactions, e.g. 100-500 mM NaCl.

Ultimately, your protein just may not be very soluble. That is potentially
OK...it will ppt and maybe xtallize well at low concentration.

Roger Rowlett
On Aug 19, 2014 1:52 PM, "Prashant Deshmukh" 
wrote:

> Hi,
> i am concentrating my protein using centricon filter, but it is
> precipitated soon. Please help me solving this problem.
> Thanks.
> Prashant Deshmukh
> Dept. of Biophysics,
> NIMHANS,
> Bangalore 560 029,
> E-mail:prashantbiophys...@gmail.com
> Mob.No.: +919620986525
>

[ccp4bb]

[Prince, D Bryan]

Dear Prashant,


I have been working with a protein-protein complex expressed in mammalian 
cells, and that complex in very poorly soluble. Even with 500mM NaCl in the 
buffer, I cannot concentrate the complex to above 3 mg/mL. I tried an old 
school technique and precipitated my protein complex with ammonium sulphate 
(~80% saturation) on ice. When I recovered my complex, I was able to get almost 
9mg/mL without any precipitation at all. The sample still crystallizes, but I 
believe now that the sulphate ion is shielding/masking part of the protein 
better than the NaCl did. Perhaps this would be worth a try for you as well?


Another thing you can try with a weakly soluble protein is to set up various 
ratios between the protein and the reservoir solution in your crystallization 
drop.


One point I have not yet seen mentioned is that some proteins are hyper 
sensitive to changes in temperature. In my opinion, any protein sample should 
be kept cold, (on ice at the bench) UNLESS you have good reason and biophysical 
data to show otherwise. If you are concentrating at room temperature, try 
concentrating at 4C if you can, you might be pleasantly surprised.


Good Luck!


Bryan Prince


From: CCP4 bulletin board  on behalf of Roger Rowlett 

Sent: Tuesday, August 19, 2014 5:50 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb]


Some things to try to increase solubility:

1. Move the buffer pH away from the expected pI. Proteins have minimum 
solubility near their pI values.
2. Add solubilizing agents to the solution, e.g., 20-50% glycerol. (This may 
alter you crystallization screening strategy)
3. Include some inert salt in the solution to minimize electrostatic 
interactions, e.g. 100-500 mM NaCl.

Ultimately, your protein just may not be very soluble. That is potentially 
OK...it will ppt and maybe xtallize well at low concentration.

Roger Rowlett

On Aug 19, 2014 1:52 PM, "Prashant Deshmukh" 
mailto:prashantbiophys...@gmail.com>> wrote:
Hi,
i am concentrating my protein using centricon filter, but it is precipitated 
soon. Please help me solving this problem.
Thanks.
Prashant Deshmukh
Dept. of Biophysics,
NIMHANS,
Bangalore 560 029,
E-mail:prashantbiophys...@gmail.com
Mob.No.: +919620986525

--
Confidentiality Notice: This message is private and may contain confidential 
and proprietary information. If you have received this message in error, please 
notify us and remove it from your system and note that you must not copy, 
distribute or take any action in reliance on it. Any unauthorized use or 
disclosure of the contents of this message is not permitted and may be unlawful.
 

[ccp4bb]

[Gloria Borgstahl]

Be aware that some buffers are temperature sensitive and change pH, if this
pH change heads toward the pI of the protein it can crash out.


On Tue, Aug 19, 2014 at 6:37 PM, Prince, D Bryan <
dbryan.pri...@astrazeneca.com> wrote:

>  Dear Prashant,
>
>
>  I have been working with a protein-protein complex expressed in
> mammalian cells, and that complex in very poorly soluble. Even with 500mM
> NaCl in the buffer, I cannot concentrate the complex to above 3 mg/mL. I
> tried an old school technique and precipitated my protein complex with
> ammonium sulphate (~80% saturation) on ice. When I recovered my complex, I
> was able to get almost 9mg/mL without any precipitation at all. The sample
> still crystallizes, but I believe now that the sulphate ion is
> shielding/masking part of the protein better than the NaCl did. Perhaps
> this would be worth a try for you as well?
>
>
>  Another thing you can try with a weakly soluble protein is to set up
> various ratios between the protein and the reservoir solution in your
> crystallization drop.
>
>
>  One point I have not yet seen mentioned is that some proteins are hyper
> sensitive to changes in temperature. In my opinion, any protein sample
> should be kept cold, (on ice at the bench) UNLESS you have good reason and
> biophysical data to show otherwise. If you are concentrating at room
> temperature, try concentrating at 4C if you can, you might be pleasantly
> surprised.
>
>
>  Good Luck!
>
>
>  Bryan Prince
>
>  --
>
> *Confidentiality Notice: *This message is private and may contain
> confidential and proprietary information. If you have received this message
> in error, please notify us and remove it from your system and note that you
> must not copy, distribute or take any action in reliance on it. Any
> unauthorized use or disclosure of the contents of this message is not
> permitted and may be unlawful.
>
>
>
>--
> *From:* CCP4 bulletin board  on behalf of Roger
> Rowlett 
> *Sent:* Tuesday, August 19, 2014 5:50 PM
> *To:* CCP4BB@JISCMAIL.AC.UK
> *Subject:* [ccp4bb]
>
>
> Some things to try to increase solubility:
>
> 1. Move the buffer pH away from the expected pI. Proteins have minimum
> solubility near their pI values.
> 2. Add solubilizing agents to the solution, e.g., 20-50% glycerol. (This
> may alter you crystallization screening strategy)
> 3. Include some inert salt in the solution to minimize electrostatic
> interactions, e.g. 100-500 mM NaCl.
>
> Ultimately, your protein just may not be very soluble. That is potentially
> OK...it will ppt and maybe xtallize well at low concentration.
>
> Roger Rowlett
> On Aug 19, 2014 1:52 PM, "Prashant Deshmukh" 
> wrote:
>
>> Hi,
>> i am concentrating my protein using centricon filter, but it is
>> precipitated soon. Please help me solving this problem.
>> Thanks.
>>  Prashant Deshmukh
>> Dept. of Biophysics,
>> NIMHANS,
>> Bangalore 560 029,
>> E-mail:prashantbiophys...@gmail.com
>> Mob.No.: +919620986525
>>
>

[ccp4bb] software for powder pattern

[Nancy Naguib]

Dear All
i would like your advise about a good software for x-ray powder diffraction. i 
used to work on a software provided from phillips but i am not anymore.
i will mainly need it for refinement for my compounds
Thanks very much
Nancy