Los últimos 2 (numero 2 y 3 en el asunto, tienen una oferta de estudio de
flagelos = flagella)
Saludos
________________________________
De: CCP4 bulletin board <CCP4BB@JISCMAIL.AC.UK> en nombre de CCP4BB automatic
digest system <lists...@jiscmail.ac.uk>
Enviado: martes, 19 de abril de 2016 06:00 p. m.
Para: CCP4BB@JISCMAIL.AC.UK
Asunto: CCP4BB Digest - 18 Apr 2016 to 19 Apr 2016 (#2016-112)
There are 15 messages totaling 2009 lines in this issue.
Topics of the day:
1. measuring the angle (2)
2. Fwd: Postdoc position available in Prof. Patti LiWang's lab at University
of California, Merced
3. Unusual diffraction (2)
4. PhaseMR - Twinning? (2)
5. FW: Postdoc opportunity at University of Texas, Austin
6. Releases of new stable versions of Global Phasing software
7. Co-crystallization with glycerophosphocholine (2)
8. X-ray Crystallography/Drug Discovery Postdoctoral Position at the
University of Georgia
9. Vacancy for a scientific data curator (PDB/EMDB) at PDBe
10. Switching projects broken?
11. Equipment and software for protein crystallization imaging and
optimization
----------------------------------------------------------------------
Date: Tue, 19 Apr 2016 02:23:34 +0000
From: Sagar Khavnekar <sagarbiophys...@gmail.com>
Subject: Re: measuring the angle
Dear Chemocev,
You can possibly do it with python.
Check this link.
https://sourceforge.net/p/pymol/mailman/message/33229437/
Else, superpose proteins for the center of mass of each subunit. Calculate
angle using rotation matrix.
I am not sure if you can superpose protein molecules so that their center
of mass coincide. Or else just superpose with lsq.
Cheers,
Sagar
On Tue 19 Apr, 2016 2:20 am chemocev marker, <jirivit...@gmail.com> wrote:
> Hi All
> I am trying to understand some protein structures and want to know how I
> can measure the angle between two subunits of heterodimer molecules.
>
> best
>
> Jiri
>
------------------------------
Date: Tue, 19 Apr 2016 02:28:11 +0000
From: Sagar Khavnekar <sagarbiophys...@gmail.com>
Subject: Re: measuring the angle
Or else just use dyndom.
http://fizz.cmp.uea.ac.uk/dyndom/
DynDom - Protein Domain Motion<http://fizz.cmp.uea.ac.uk/dyndom/>
fizz.cmp.uea.ac.uk
DynDom is a program to determine domains, hinge axes and hinge bending residues
in proteins where two conformations are available
On Tue 19 Apr, 2016 7:53 am Sagar Khavnekar, <sagarbiophys...@gmail.com>
wrote:
> Dear Chemocev,
>
> You can possibly do it with python.
>
> Check this link.
> https://sourceforge.net/p/pymol/mailman/message/33229437/
>
> Else, superpose proteins for the center of mass of each subunit. Calculate
> angle using rotation matrix.
>
> I am not sure if you can superpose protein molecules so that their center
> of mass coincide. Or else just superpose with lsq.
>
> Cheers,
>
> Sagar
>
> On Tue 19 Apr, 2016 2:20 am chemocev marker, <jirivit...@gmail.com> wrote:
>
>> Hi All
>> I am trying to understand some protein structures and want to know how I
>> can measure the angle between two subunits of heterodimer molecules.
>>
>> best
>>
>> Jiri
>>
>
------------------------------
Date: Mon, 18 Apr 2016 23:16:17 -0400
From: Steve Chou <stevezc...@gmail.com>
Subject: Fwd: Postdoc position available in Prof. Patti LiWang's lab at
University of California, Merced
Dear CCP4BB subscribers,
I'm posting this ad on behalf of Prof. Patti LiWang. A postdoc position is
open in her lab at University of California, Merced. See the info below for
details. The position represents an excellent opportunity for researchers
to develop their careers. Interested and qualified individuals can apply
through the following official link.
All the best,
Steve
https://aprecruit.ucmerced.edu/apply/JPF00346
<https://urldefense.proofpoint.com/v2/url?u=https-3A__aprecruit.ucmerced.edu_apply_JPF00346&d=AwMGaQ&c=-dg2m7zWuuDZ0MUcV7Sdqw&r=VF0xyZ0LE6U5N6N8rq9eKSI-50_TqK5CYlRZ4hr_nMA&m=yapq0HMu7rtRTWqqUsfIji9raZuPl_bhaSbJBGKyIlo&s=tu5b5O8Z1twWZXpvzfTFS51NHOpVqJ0ImePeHvrokNg&e=>
*Open date: *April 18th, 2016
*Next review date: *May 18th, 2016
Apply by this date to ensure full consideration by the committee.
*Final date: *May 18th, 2016
Applications will continue to be accepted until this date, but those
received after the review date will only be considered if the position has
not yet been filled.
DESCRIPTION
A Postdoctoral Scholar position is available in the biochemical and
biophysical research lab at the University of California, Merced. This
position primarily involves carrying out biochemical research on proteins
to study inflammation and HIV inhibition. This work will include protein
expression and purification from multiple sources such as E. coli, yeast,
and mammalian cells; Molecular biology such mutagenesis and ELISA assays;
Mammalian cell culture and biological assays including binding and
single-round virus infectivity assays. Research may also include
biophysical techniques such as NMR, fluorescence, and isothermal titration
calorimetry.
Required Qualifications: Successful applicants will have a PhD in
Biochemistry, or relevant experience in related fields, and a willingness
to learn a variety of techniques.
Preferred Qualifications: Interested candidates to have experience in
carrying out biochemical research on proteins to study inflammation and HIV
inhibition.
Situated near Yosemite National Park, UC Merced is a dynamic new
university, which opened in September 2005 as the tenth campus of the
University of California and the first American research university in the
21st century. Biochemistry faculty and students enjoy a highly
collaborative research environment, while building excellence in
biophysical research, and contributing to the development of a Public
Health program. Biochemical health research is supported through the Health
Sciences Research Institute, the largest organized research unit on campus.
Interested individuals should submit 1) a cover letter describing research
experiences and interests, and career goals, 2) curriculum vitae, 3) a list
of two references with contact information including mailing address, phone
number and email address, and 4) up to two relevant (p)reprints.
Initial review of applications will begin immediately. Recruitment will
remain open until position is filled, with a closing date of May 18, 2016.
For questions and more information, please contact Professor Patricia
LiWang, Ph.D. at pliw...@ucmerced.edu. The University of California, Merced
is an affirmative action/equal opportunity employer with a strong
institutional commitment to the achievement of diversity among its faculty,
staff, and students.
Salary is based on the University of California Academic Postdoctoral
Scholar Salary scale.
The University of California, Merced is an affirmative action/equal
opportunity employer with a strong institutional commitment to the
achievement of diversity among its faculty, staff, and students.
JOB LOCATION
Merced, CA
REQUIREMENTS DOCUMENTS
-
Curriculum Vitae - Your most recently updated C.V.
-
Cover Letter - Describe research experiences and interests, and career
goals.
-
Reference and Contact Information - A list of two references with
contact information including mailing address, phone number and email
address.
-
Reprints - Up to two relevant (p)reprints.
REFERENCES
2-5 letters of reference required
HOW TO APPLY
1. Create an ApplicantID
2. Provide required information and documents
3. If any, provide required reference information
*Get started: press Apply Now*
Cheers,
Patti LiWang
Patricia LiWang
Professor, Molecular Cell Biology
University of California Merced
pliw...@ucmerced.edu
Post doc position available: https://aprecruit.ucmerced.edu/apply/JPF00346
<https://urldefense.proofpoint.com/v2/url?u=https-3A__aprecruit.ucmerced.edu_apply_JPF00346&d=AwMGaQ&c=-dg2m7zWuuDZ0MUcV7Sdqw&r=VF0xyZ0LE6U5N6N8rq9eKSI-50_TqK5CYlRZ4hr_nMA&m=yapq0HMu7rtRTWqqUsfIji9raZuPl_bhaSbJBGKyIlo&s=tu5b5O8Z1twWZXpvzfTFS51NHOpVqJ0ImePeHvrokNg&e=>
------------------------------
Date: Tue, 19 Apr 2016 09:56:14 +0100
From: John R Helliwell <jrhelliw...@gmail.com>
Subject: Re: Unusual diffraction
Hi,
Just to also mention for you to check your successive diffraction images
through the whole crystal sample rotation.
Thus far I note the general absence of diffuse streaking in the example
diffraction images, which is at least a 'simplification'.
Best wishes,
John
On Mon, Apr 18, 2016 at 4:18 PM, Jarrod Mousa <jjmo...@gmail.com> wrote:
> Dear community,
>
> I collected data from a crystal grown in 30% PEG 8000, 200 mM ammonium
> sulfate, 100 mM sodium cacodylate pH 6.4 and 40% v/v Pentaerythritol
> ethoxylate (3/4 EO/OH), and cryoprotected with 20% glycerol. I am attaching
> a snapshot of the diffraction pattern along with a zoomed in portion. I am
> having trouble solving by molecular replacement, even though I have a very
> good starting model. Just wanted to get people's insights into the odd (at
> least to me) diffraction pattern. The data can process with XDS in P 4 2 2.
> I also attached merging statistics.
>
> Thank you,
>
> Jarrod Mousa
> Post-doctoral research fellow
> Crowe Laboratory
> Vanderbilt University Medical Center
>
>
--
Professor John R Helliwell DSc
------------------------------
Date: Tue, 19 Apr 2016 18:23:38 +0900
From: Takanori Nakane <takanori.nak...@bs.s.u-tokyo.ac.jp>
Subject: Re: Unusual diffraction
Hi Jarrod,
Creating a pseudo-precession image with
labelit.precession_photo would be informative.
The program is described in Nick Sauter's article in
Computational Crystallography Newsletter 2011 Jan.
My program called "dials.rs_mapper", which is included in DIALS,
can reconstruct the reciprocal space and outputs in CCP4 map format.
Then you can volume-render the output in PyMOL.
Best regards,
Takanori Nakane
Am 2016年04月19日 um 17:56 schrieb John R Helliwell:
> Hi,
> Just to also mention for you to check your successive diffraction images
> through the whole crystal sample rotation.
> Thus far I note the general absence of diffuse streaking in the example
> diffraction images, which is at least a 'simplification'.
> Best wishes,
> John
>
> On Mon, Apr 18, 2016 at 4:18 PM, Jarrod Mousa <jjmo...@gmail.com
> <mailto:jjmo...@gmail.com>> wrote:
>
> Dear community,
>
> I collected data from a crystal grown in 30% PEG 8000, 200 mM
> ammonium sulfate, 100 mM sodium cacodylate pH 6.4 and 40% v/v
> Pentaerythritol ethoxylate (3/4 EO/OH), and cryoprotected with 20%
> glycerol. I am attaching a snapshot of the diffraction pattern along
> with a zoomed in portion. I am having trouble solving by molecular
> replacement, even though I have a very good starting model. Just
> wanted to get people's insights into the odd (at least to me)
> diffraction pattern. The data can process with XDS in P 4 2 2. I
> also attached merging statistics.
>
> Thank you,
>
> Jarrod Mousa
> Post-doctoral research fellow
> Crowe Laboratory
> Vanderbilt University Medical Center
>
>
>
>
> --
> Professor John R Helliwell DSc
------------------------------
Date: Tue, 19 Apr 2016 19:32:03 +0800
From: Sam Tang <samtys0...@gmail.com>
Subject: PhaseMR - Twinning?
Hello,
I am carrying out molecular replacement on one of our recent data set using
Phaser-MR. The data set was indexed P1 to 2.5 Angstorm. In my initial run,
Phaser-MR returned the following:
--------
TWINNING
--------
tNCS/Twin Detection Table
-------------------------
-Second Moments- --P-values--
Centric Acentric untwinned twin frac
<5%
Theoretical for untwinned 3.00 2.00
Theoretical for perfect twin 2.00 1.50
Initial (data as input) 0.00 2.41+/-0.070 1 1
After Anisotropy Correction 0.00 2.12+/-0.052 1 1
After Anisotropy and tNCS ---n/a---
P-value < 0.01 for <5% twinned is considered significant
Resolution for Twin Analysis (85% I/SIGI > 3): 3.54A (HiRes= 2.67A)
Afterward the initial run I tried to re-run the job keeping all input mtz
and model pdb and other parameters the same. (I simply click 'ReRun job' on
the menu.) The only adjustments were (1) ensemble IDENT from 90% to 95%;
(2) No. of copies to search for from 2 to 1. This time the programme warns
of significant twinning:
--------
TWINNING
--------
tNCS/Twin Detection Table
-------------------------
-Second Moments- --P-values--
Centric Acentric untwinned twin frac
<5%
Theoretical for untwinned 3.00 2.00
Theoretical for perfect twin 2.00 1.50
Initial (data as input) 0.00 1.35+/-0.013 0 0
After Anisotropy Correction 0.00 1.29+/-0.011 0 0
After Anisotropy and tNCS ---n/a---
P-value < 0.01 for <5% twinned is considered significant
Resolution for Twin Analysis (85% I/SIGI > 3): 3.15A (HiRes= 2.67A)
-------------------------------------------------------------------------------------
Warning: Intensity moments suggest significant twinning (>5%). Tests based
on
possible twin laws will be more definitive.
-------------------------------------------------------------------------------------
To my understanding Phaser first treats the data for twin / not twin before
it really puts in the model. Thus I am curious why the same set of input
data and model give different results in Twinning test?
Thanks!
Sam
PhD Candidate, The Chinese University of Hong Kong
------------------------------
Date: Tue, 19 Apr 2016 12:51:26 +0000
From: "Keller, Jacob" <kell...@janelia.hhmi.org>
Subject: Re: PhaseMR - Twinning?
If you processed your data in Aimless, the log file will contain much more
information about twinning. Try looking there.
From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of Sam Tang
Sent: Tuesday, April 19, 2016 7:32 AM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] PhaseMR - Twinning?
Hello,
I am carrying out molecular replacement on one of our recent data set using
Phaser-MR. The data set was indexed P1 to 2.5 Angstorm. In my initial run,
Phaser-MR returned the following:
--------
TWINNING
--------
tNCS/Twin Detection Table
-------------------------
-Second Moments- --P-values--
Centric Acentric untwinned twin frac <5%
Theoretical for untwinned 3.00 2.00
Theoretical for perfect twin 2.00 1.50
Initial (data as input) 0.00 2.41+/-0.070 1 1
After Anisotropy Correction 0.00 2.12+/-0.052 1 1
After Anisotropy and tNCS ---n/a---
P-value < 0.01 for <5% twinned is considered significant
Resolution for Twin Analysis (85% I/SIGI > 3): 3.54A (HiRes= 2.67A)
Afterward the initial run I tried to re-run the job keeping all input mtz and
model pdb and other parameters the same. (I simply click 'ReRun job' on the
menu.) The only adjustments were (1) ensemble IDENT from 90% to 95%; (2) No. of
copies to search for from 2 to 1. This time the programme warns of significant
twinning:
--------
TWINNING
--------
tNCS/Twin Detection Table
-------------------------
-Second Moments- --P-values--
Centric Acentric untwinned twin frac <5%
Theoretical for untwinned 3.00 2.00
Theoretical for perfect twin 2.00 1.50
Initial (data as input) 0.00 1.35+/-0.013 0 0
After Anisotropy Correction 0.00 1.29+/-0.011 0 0
After Anisotropy and tNCS ---n/a---
P-value < 0.01 for <5% twinned is considered significant
Resolution for Twin Analysis (85% I/SIGI > 3): 3.15A (HiRes= 2.67A)
-------------------------------------------------------------------------------------
Warning: Intensity moments suggest significant twinning (>5%). Tests based on
possible twin laws will be more definitive.
-------------------------------------------------------------------------------------
To my understanding Phaser first treats the data for twin / not twin before it
really puts in the model. Thus I am curious why the same set of input data and
model give different results in Twinning test?
Thanks!
Sam
PhD Candidate, The Chinese University of Hong Kong
------------------------------
Date: Tue, 19 Apr 2016 14:16:24 +0000
From: "Zhang, Yan" <jzh...@cm.utexas.edu>
Subject: FW: Postdoc opportunity at University of Texas, Austin
Hi, everyone:
I am posting this for a colleague of mine. Please contact her directly about
the position.
Structural Biology Post-doctoral positions available for investigating
flagellar motor function/ role in surface sensing / swarming motility and
antibiotic resistance using E. coli/Salmonella/Vibrio cholera. These subjects
will be explored using genetics, biochemistry, cell biology and structural
biology. The projects are exciting not only for elucidating fundamental
mechanisms in biology but for potential applications in therapeutics as well.
Applicants must have first-author publications in peer-reviewed journals and be
highly motivated. A strong background in bacterial genetics, physiology and
biochemistry is preferred. Proficiency with protein purification and
crystallization is strongly desired. A basic understanding of programming and
network analysis is a plus.
Austin, TX has been consistently ranked one of the best places to live in the
United States. The University of Texas offers competitive benefits. Applicants
should email their CV and list of three references directly to Rasika Harshey:
ras...@austin.utexas.edu
https://sites.cns.utexas.edu/harsheylab
------------------------------
Date: Tue, 19 Apr 2016 15:54:02 +0100
From: Gerard Bricogne <g...@globalphasing.com>
Subject: Releases of new stable versions of Global Phasing software
Dear CCP4 users,
We are pleased to announce new stable releases of all our software
packages: SHARP/autoSHARP (for experimental phasing), autoPROC (for
automated processing and analysis of diffraction data) and BUSTER (for
maximum-likelihood structure refinement, with added functionalities
for handling target-ligand complexes). They are fully compatible with
the latest CCP4 release, and are available free of charge to academic
users.
For licence requests, installation instructions, documentation and
download information, please connect to our Web server at
http://www.globalphasing.com/sharp
http://www.globalphasing.com/autoproc
http://www.globalphasing.com/buster
We have simplified our licensing scheme so that it is sufficient to
have a single licence key in order to run on multiple machines.
In addition to the BUSTER refinement program itself, the BUSTER
package also includes
* buster-report, which generates a graphical analysis, in both html
and pdf formats, of the outcome of a BUSTER refinement;
* Grade, a small-molecule (ligand) restraint dictionary generator;
* Rhofit, our automated ligand fitter; and
* Pipedream, which links autoPROC, BUSTER and Rhofit to provide an
automated fragment/ligand screening pipeline.
These new stable releases contain multiple new features, performance
enhancements and improvements.
Amongst the highlights are:
SHARP/autoSHARP:
* Support for the latest versions of CCP4, SHELX and ARP/wARP.
* Command-line interface to autoSHARP (in addition to the existing
CCP4i task and to the httpd-based interface for SHARP/autoSHARP).
This simplifies automation and inclusion into pipelines.
* Log-likelihood gradient ("residual") maps can now be read directly
into Coot via their MTZ files (i.e. as amplitudes and phases).
* Improved decision-making regarding automatic building with BUCCANEER
and/or ARP/wARP.
autoPROC:
* Addition of an image viewer (gpx2) and prediction generator
(simcal_predict) to provide a capability to simultaneously view
images, spots, and predictions of spot positions and shapes based on
various indexing solutions;
* Addition of support for new detector types (e.g. Pilatus and Eiger),
for more beamlines and lab-source setups, and for reading Eiger hdf5
files.
* Support for new scaling paths, including a pure-AIMLESS path and an
XSCALE path.
* Generation of a summary HTML page presenting the processing results,
including both statistical and graphical information to inform the
user on the outcome of processing.
* Analysis of "early-minus-late" trends in the data and, whenever
possible, production of difference coefficients to help visualise
the effects of radiation damage.
* Capability to write an ISPyB-compatible XML file for incorporation
into a synchrotron workflow.
BUSTER:
* Improvements in buster-report, which now reports its analysis of
ligand geometry both in html and pdf output.
* Improved handling of glycoprotein and polysaccharide linkages in
BUSTER.
* Major reworking of geometry checks, including the initial sanity
check and disulfide bonds.
* Improvements in the speed of execution of BUSTER for very large
structures such as ribosomes.
* Added facility to calculate F(early) - F(late) difference Fourier
maps and anomalous difference Fourier maps, when applicable.
* Support for multiple input models in Pipedream to accommodate
conformational changes induced by ligand binding, with automatic
selection of the model that best matches the input data.
* Support for ligand database (e.g. corporate) identifiers in Grade
and buster-report.
For a full list of changes and updates, please see the Release Notes
for the individual packages via the corresponding News pages at
http://www.globalphasing.com/sharp/news.html
http://www.globalphasing.com/autoproc/news.html
http://www.globalphasing.com/buster/news.html
With best wishes - the Global Phasing Developers:
Claus Flensburg, Peter Keller, Wlodek Paciorek, Andrew Sharff,
Clemens Vonrhein and Gerard Bricogne
------------------------------
Date: Tue, 19 Apr 2016 20:25:40 +0530
From: monika chandravanshi <chandravanshi.monik...@gmail.com>
Subject: Co-crystallization with glycerophosphocholine
Dear All,
Has anybody tried to co-crystallize the glycerophosphocholine
with protein?
Thank you,
Monika Chandravanshi
------------------------------
Date: Tue, 19 Apr 2016 13:34:49 -0400
From: Scott Pegan <scott.d.pe...@gmail.com>
Subject: X-ray Crystallography/Drug Discovery Postdoctoral Position at the
University of Georgia
Seeking Post-Doctoral candidates for a newly funded position in my
laboratory located in the University of Georgia's College of Pharmacy. This
individual will assist in my federally funded related projects that involve
the use of molecular biology, protein purification, enzymology, structural
biology (X-ray) as well as other drug discovery and biophysical techniques.
Project related fields include infectious disease, structure-based drug
design. My laboratory, and UGA at large, possesses significant structural
biology and protein science resources including a robust wet lab
infrastructure, a brand new X-ray home source, the latest in crystallization
robotics, liquid handling robots and regular access to the SER-CAT at APS.
More information on my laboratory can be found at: http://pbs.rx.uga.edu/
scott-pegan-ph-d-associate-professor/
Recent graduates with X-ray crystallography experience encouraged. A track
record with expressing/refolding recombinant proteins and/or performing
enzymology will be a plus. Ideal start date would be the June-August time
frame. Also, preference will be given to those applicants with one, or more
first author publications. Compensation will be commensurate with
experience and range from $40,000-$48,000. Interested parties please send a
single PDF file with your CV, with publication list included, and a minimum
of two references. Please submit to spe...@uga.edu.
------------------------------
Date: Tue, 19 Apr 2016 21:15:20 +0200
From: Gerard DVD Kleywegt <ger...@xray.bmc.uu.se>
Subject: Vacancy for a scientific data curator (PDB/EMDB) at PDBe
Hi all,
Are you a structural biologist looking for an exciting career change in 2016?
We are looking to recruit an expert structural biologist (with experience in
structure determination) to join the Protein Data Bank in Europe curation team
(PDBe: pdbe.org) at the European Bioinformatics Institute (EMBL-EBI,
Cambridge, UK: ebi.ac.uk) as a Scientific Data Curator. The work involves
annotating preliminary PDB and Electron Microscopy Data Bank (EMDB)
submissions and extracting relevant biological information. In addition,
curators contribute to training, outreach and user-support activities of PDBe
and the EMBL-EBI.
For more information, please go to:
http://www.embl.de/jobs/searchjobs/index.php?ref=EBI_00715
To see some of your potential future colleagues, as well as some of our recent
publications, please surf to:
http://www.ebi.ac.uk/about/people/gerard-kleywegt
Feel free to pass the information on to any potentially interested and
qualified people you may know.
Thanks!
--Gerard
---
Gerard J. Kleywegt, PDBe, EMBL-EBI, Hinxton, UK
ger...@ebi.ac.uk ..................... pdbe.org
Secretary: Pauline Haslam pdbe_ad...@ebi.ac.uk
------------------------------
Date: Tue, 19 Apr 2016 21:02:44 +0000
From: "Keller, Jacob" <kell...@janelia.hhmi.org>
Subject: Switching projects broken?
Dear CCP4 developers, sorry to bother you again, but after restarting and
head-scratching, I am still getting this error msg when I try to switch to a
certain project. Any idea what to do about it? Can the database be edited
manually to take out the offending entry, perhaps?
Jacob Keller
can't read "database(TITLE,161)": no such element in array
can't read "database(TITLE,161)": no such element in array
while executing
"append [subst $item] $database($item,[subst $job_id]) " ""
(procedure "DbJobDescription" line 33)
invoked from within
"DbJobDescription $project $job_id $display $display_format"
(procedure "FeedListbox" line 17)
invoked from within
"FeedListbox $frame $job_list $db_display $db_display_format"
(procedure "db_update_list" line 31)
invoked from within
"db_update_list $project $db_display $db_display_format $no_jobs_message "
(procedure "DbUpdateList" line 16)
invoked from within
"DbUpdateList"
(procedure "DbOpen" line 76)
invoked from within
"DbOpen"
(procedure "DbChangeFile" line 37)
invoked from within
"DbChangeFile $project"
(procedure "SwitchProject" line 9)
invoked from within
"SwitchProject Twin1_9 .module.mesbar.switchProj.m"
(menu invoke)
*******************************************
Jacob Pearson Keller, PhD
Looger Lab/HHMI Janelia Research Campus
19700 Helix Dr, Ashburn, VA 20147
email: kell...@janelia.hhmi.org
*******************************************
------------------------------
Date: Tue, 19 Apr 2016 23:33:13 +0200
From: chemocev marker <jirivit...@gmail.com>
Subject: Re: Co-crystallization with glycerophosphocholine
There is a crystal structure with phosphocholine 5EGH
On Tue, Apr 19, 2016 at 4:55 PM, monika chandravanshi <
chandravanshi.monik...@gmail.com> wrote:
> Dear All,
>
> Has anybody tried to co-crystallize the glycerophosphocholine
> with protein?
>
>
>
> Thank you,
> Monika Chandravanshi
>
>
>
>
>
------------------------------
Date: Tue, 19 Apr 2016 21:28:25 +0000
From: "Leonard,Paul" <pleona...@mdanderson.org>
Subject: Equipment and software for protein crystallization imaging and
optimization
Hi,
Can anyone recommend equipment for
1. Setting up crystallization trials. (I'm familiar with Art Robbins
Gryphon/Phoenix, TPP labtech Mosquito/Dragonfly and Formulatrix NT8/Formulator
systems so I'm specifically interested in knowing if there are other companies
developing alternatives).
2. Drop imaging equipment. (I'm familiar with systems from Formulatrix and
Rigaku - any other systems people like?)
3. Software for managing crystallization trials. (I'm familiar with RockMaker
from Formulatrix. Any other players?)
4. Any imaging systems for detecting crystals in an automated way?
Thank-you for any help you can provide.
Kind regards,
Paul
Instructor
MD Anderson Cancer Center
Email: pleona...@mdanderson.org
The information contained in this e-mail message may be privileged,
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protected health information (PHI); dissemination of PHI should comply with
applicable federal and state laws. If you are not the intended recipient, or an
authorized representative of the intended recipient, any further review,
disclosure, use, dissemination, distribution, or copying of this message or any
attachment (or the information contained therein) is strictly prohibited. If
you think that you have received this e-mail message in error, please notify
the sender by return e-mail and delete all references to it and its contents
from your systems.
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End of CCP4BB Digest - 18 Apr 2016 to 19 Apr 2016 (#2016-112)
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