[ccp4bb] 5th Annual SER-CAT symposium - March 7th - Charleston, SC

[Chris Davies]

For those interested, the 5th Annual SER-CAT Symposium will be held on March
7th 2008 in Charleston, SC, USA.

SER-CAT is a consortium of mostly Southeast US-based institutions that
operates Sector 22 at the Advanced Photon Source.  The one-day meeting
highlights interesting structures arising from use of the SER-CAT beam
lines, but also includes talks describing new methods for crystal structure
determination, as well as recent developments on the beam lines.

The deadline for registration is February 22nd.  (The deadline to get the
conference rate at the hotel is February 12th, i.e. tomorrow).

For more information, please visit the conference web site at:
http://biochemistry.musc.edu/ser-cat/

Thanks
Chris Davies

*
Christopher Davies, Ph. D.,
Associate Professor,
Dept. of Biochemistry & Molecular Biology,
Medical University of South Carolina,
Charleston SC 29425 USA.
(843) 792 1468

Re: [ccp4bb] Does NCS bias a randomly-chosen test set (even if not enforced)?

[Edward Berry]

Dirk Kostrewa wrote:

Dear Ed,

although, I don't think that a comparison of refinement in a higher and 
a lower symmetry space group is valid for general NCS cases, I will try 
to answer your question. Here are my thoughts for two different cases:


(1) You have data to atomic resolution with high I/sigma and low Rsym (I 
assume high redundancy). The n copies of the asymmetric unit in the unit 
cell are really identical and obey the higher symmetry (so, not a 
protein crystal). When you process the data in lower symmetry (say, P1), 
the non-averaged "higher-symmetry"-equivalent Fobs will differ due to 
measurement errors, and thus reflections in the working-set will differ 
to "higher-symmetry"-related reflections in the test-set due to these 
measurement errors. If you then refine the n copies against the 
working-set in the lower P1 symmetry, you minimize |Fobs(work)-Fcalc|, 
resulting in Fcalcs that become closer to the working-set Fobs. As a 
consequence, the Fcalcs will thus diverge somewhat from the test-set 
Fobs. However, since this atomic model is assumed to be very well 
defined obeying the higher symmetry, and, furthermore, the working-set 
contains well measured "higher-symmetry"-equivalent Fobs, the resulting 
atomic positions, and thus the Fcalcs, will be very close to their 
equivalent values in the higher-symmetry refinement. Therefore, the 
Fcalcs will also be still very similar to the 
"higher-symmetry"-equivalent Fobs in the test-set, and I would expect a 
difference between Rwork and Rfree ranging from "0" to the value of 
Rsym. In other words, the Fobs in the test-set are not really 
independent of the reflections in the working-set, and thus Rfree is 
heavily biased towards Rwork.
In this case, I would not expect large differences in the outcome due to 
the additional application of "NCS"-constraints/restraints.


As I see it, this is clearly a case of |Fo-Fc| for the test reflectins
decreasing because the model is getting better, and there is no bias.
Lets say the higher symmetry really does apply, so the correct structure
is perfectly symmetrical and the "NCS-related" reflections agree to within
the error level.
Lets also say the initial model is perfectly symmetrical (you solved the
molecular replacement with two copies of the same monomer, and rigid-
body refinement positioned them exactly). But let's say it is completely
unrefined- the search model is from a different organism in a different
space group, and modified by homology modeling to your sequence.
So the Fo obey the  NCS within error, The Fc obey the NCS, but the
Fobs don't fit the Fcalc very well. Initially there is no Free-R bias,
because the model has not been refined agaist the data. The free set
can only be biased by refinement, since it is only during refinement
that the the free set is treated differently. Thus it doesn't matter
that the ncs-related Fo are correlated and the ncs-related Fc
are correlated: it is only the CHANGES in Fc that could introduce
model bias, and they are uncorrelated if you do not enforce ncs.

Now as we refine, the model will converge toward the correct symmetrical
model as a result of minimizing the |Fo-Fc| for the work reflections.
At the same time the |Fo-Fc| for the test reflections will also decrease
on the average, but to a lesser extent. I argue that the only mechanism
for refinement to reduce |Fo-Fc| at a test reflection is by improving
the structure, and I think that constitutes an unbiased Free-R value.

If you can think of any mechanism to reduce |Fo-Fc| for a test reflection
because you are refining against a symm-related work reflection, then
the R-free would be biased.  This is not the case if you do not enforce
symmetry. On the average no decrease in |Fo-Fc|(test) will result from
changes that reduce |Fo-Fc| for the work reflection: given an arbitrary
change in the structure, the change in |Fc| at arbitrary reflections
is a pseudo-random variable with expected value zero, and there is no
correlation between the change at ncs-related reflections.

The value of |Fo-Fc| at a test reflection goes down, not due to
changes which improve the fit at a sym-related working reflection,
but because of changes that improve the fit at all test reflections,
and then only because the structure is improving. The atoms moved into
symmetrical positions not because they were constrained to do so,
but because that fits the data better, in turn because the true structure
is symmetrical. If the symmetry doesn't hold for some atoms, they will
tend to move into asymmetric positions to minimize |Fo-Fc| at work
reflections, now *decreasing* the correlation with sym-related work
reflections. But again this will tend to reduce |Fo-Fc| at free
reflections, simply because the model is better approximating the
true structure.

To make a more obvious parallel, suppose you are refining a low-resolution
dataset from a microcrystal (with no NCS). In another directory on the
same disk you have a high resoluti

Re: [ccp4bb] shipping heavy-atom solutions using Fedex

[Chavas Leo]

Dear David,

I'm not sure, but you might find something useful there:
www.sddc.army.mil/sddc/ Content/Pub/11467/Attachment3.pdf

HTH


Kind regards.

Leo

Chavas Leonard, Ph.D.
Research Associate

Faculty of Life Sciences
The University of Manchester
The Michael Smith Building
Oxford Road
Manchester Lancashire
M13 9PT

Tel: +44(0)161-275-1586
e-mail: [EMAIL PROTECTED]

Re: [ccp4bb] an over refined structure

[Bart Hazes]

Dale Tronrud wrote:

Bart Hazes wrote:


Dale Tronrud wrote:


[EMAIL PROTECTED] wrote:
 > Rotational near-crystallographic ncs is easy to handle this way, but
 > what about translational pseudo-symmetry (or should that be
 > pseudo-translational symmetry)? In such cases one whole set of 
spots is

 > systematically weaker than the other set.  Then what is the
 > "theoretically correct" way to calculate Rfree?  Write one's own 
code to

 > sort the spots into two piles?
 > Phoebe
 >

Dear Phoebe,

   I've always been a fan of splitting the test set in these situations.
The weak set of reflections provide information about the differences
between the ncs mates (and the deviation of the ncs operator from a
true crystallography operator) while the strong reflections provide
information about the average of the ncs mates.  If you mix the two
sets in your Rfree calculation the strong set will tend to dominate
and will obscure the consequences of allowing you ncs mates too much
freedom to differ.



I haven't had to deal with this situation but my first impression is 
to use the strong reflections for Rfree. For the strong reflections, 
and any normal data, Rwork & Rfree are dominated by model errors and 
not measurement errors. For the weak reflections measurement errors 
become more significant if not dominant. In that case Rwork & Rfree 
will not be a sensitive measure to judge model improvement and 
refinement strategy.


A second and possibly more important issue arises with determination 
of Sigmaa values for maximum likelihood refinement. Sigmaa values are 
related to the correlation between Fc and Fo amplitudes. When half of 
your observed data is systematically weakened then this correlation is 
going to be very high, even if the model is poor or completely wrong, 
as long as it obeys the same pseudo-translation. If you only use the 
strong reflections for Rfree I expect that should get around some of 
the issue.


Of course it can be valuable to also monitor the weak reflections to 
optimize NCS restraints but probably not to drive maximum likelihood 
refinement or to make general refinement strategy choices.


Bart


Dear Bart,

   I agree that the way one uses the test set depends critically on the
question you are asking.  In my letter I was focusing on that aspect
of the pseudo centered crystal problem where the strong/weak divide can
be used to particular advantage.

   I have not thought as much about the matter of using the test set
to estimate the level of uncertainty in the parameters of a given model.
My gut response is that the strong/weak distinction is still significant.
Since the weak reflections contain information about the differences
between the two, ncs related, copies I suspect that a great many systematic
"errors" are subtracted out.

   For example, if your model contains isotropic B's when, of course,
the atoms move anisotropically, your maps will contain difference features
due to these unmodeled motions.  Since the anisotropic motions are
probably common to the two molecules, these features will be present in
the average structure described by the strong reflections but will be
subtracted out in the "difference" structure described by the weak
reflections.  This argument implies to me that the strong reflections
need to be judged by the Sigma A derived from the strong test set and
the weak reflections judged by the weak test set.

Dale Tronrud


Hi Dale, I agree with the above but think there is yet another way to 
think about this which may also suggest a more general solution.


In a case of pseudo-translational NCS you can separate three effects.

1) An overal modulation of reflection intensity that depends just on the 
pseudo translation vector (x,y,z) and the reflection indices (h,k,l).
2) Deviations from pure translation due to the NCS axis not being 
perfectly parallel to the crystallographic axis.
3) Deviations from pure translation due to local structural deviations 
between NCS-related molecules.


The problems I was referring to are due to the first effect, which 
messes up the expected structure factor intensity distribution. Your 
comments relate to the second and especially third effects where the 
weak reflections inform about actual differences between the NCS-related 
molecules.


Sigmaa calculations already correct for expected intensity effects due 
to crystallographic symmetry but not for pseudo-translation effects. 
Given the translation component of the pseudotranslational symmetry it 
is possible to estimate the expected intensity for a reflection and I 
would think that could be used as a correction factor just like we do 
with normal crystallographic symmetry. This correction would basically 
transform the bimodal intensity distribution due to strong and weak 
subsets of reflections back to a normal unimodal distribution which, in 
an ideal world, only differs from normal data in the fact that the weak 
subset will have a poor F/SigF ratio comp

Re: [ccp4bb] Protein-protein docking

[Walter Novak]

Hi Josiah,

You could also try ClusPro. Very quick and easy. http://nrc.bu.edu/cluster/

Best,
Wally

On Feb 11, 2008, at 2:14 AM, [EMAIL PROTECTED] wrote:


Hi all,

Can anyone tell me what programs are available to do protein-protein  
docking?


Thanks in advance,

Regards,
Josiah.



Walter R.P. Novak, Ph.D.
Postdoctoral Fellow
Rosenstiel Basic Medical Research Center
Brandeis University
415 South St. MS 029
Waltham, MA 02454-9110
Phone: (781) 736-4944
Fax: (781) 736-2405

[ccp4bb] Protein crystallography position at Sussex University

[Darren Thompson]

Postdoctoral Research Assistant in Protein Crystallography 
Ref: 131



Applications are invited for a three year Postdoctoral position, funded by 
the MRC, in the laboratory of Dr. Darren Thompson, University of Sussex, 
Brighton.  The successful candidate will work on the Complement component 
C1. The Complement system is part of the innate immune system and is 
implicated in such conditions as arthritis and heart disease. The aim of 
the project is to determine the structure of this complex and investigate 
its stability and activity. The work will involve the use of X-ray 
crystallography, E.M, fluorescence and DLS.


Applicants should have appropriate degrees and experience in protein 
biochemistry and protein crystallography.  Salary will be within the range 
£24,403 - £27,466 per annum, depending on qualifications and experience. 
This post is available immediately and will be offered on a fixed term 
contract for a period of 3 years.


Please direct informal enquiries to Dr. Darren Thompson: 
[EMAIL PROTECTED]


Closing date for applications: 8th March 2008

For full details and how to apply see www.sussex.ac.uk/jobs

Application details are available from and should be returned to Human 
Resources, Sussex House, University of Sussex, Falmer, Brighton BN1 9RH. 
Tel: (01273) 678706, fax: (01273) 877401, Email: [EMAIL PROTECTED] 
Details of all posts can also be found via  www.sussex.ac.uk/jobs


Please quote ref: 131

[ccp4bb] shipping heavy-atom solutions using Fedex

[David Aragao]

Dear All,

We need to ship small amounts (< 100ul, [ ] < 5mM) of heavy atom (HA) 
solutions to a synchrotron for onsite HA soaking. Fedex is able to do so 
but is asking for the corresponding UN numbers. All the HAs are from 
Hampton Research kit. We have found the UN number for three HA but we 
cannot find for the other 3. Does anyone has experience in shipping 
these compounds or knows where we could get these numbers for:


ethyl mercuric phosphate (EMP) - C2H5HgO)HPO2
potassium tetranitroplatinate - K2Pt(NO2)4
potassium tetracyanoplatinate - K2Pt(CN)4

We are thinking in leaving EMP out but to ship the above platinum HAs 
with the same UN number as K2PtCl4 (UN 3288.61 toxic solid, inorganic).


any comment would be extremely useful,

Thanks in advance,

David
---
David platinum, Ph. D.
Postdoctoral Researcher
Membrane Structural and Functional Biology group
CES department, University of Limerick
Ireland

Re: [ccp4bb] Protein-protein docking

[Andreas Förster]

Hey Josiah,

if you're into self-flagellation, try RosettaDock 
(http://www.rosettacommons.org/software/).  The program is viciously 
obfuscated and the learning curve correspondingly steep, but once you've 
figured things out, it's quite powerful.  Take the published protocols 
with a grain of salt, follow the tutorial on the web instead.  For best 
effect, it helps to have roomful of CPUs idling somewhere.



Andreas


[EMAIL PROTECTED] wrote:

Hi all,

Can anyone tell me what programs are available to do protein-protein docking?

Thanks in advance,

Regards,
Josiah.

[ccp4bb] Machine Learning in Structural Bioinformatics conference, Copenhagen, April 23rd 2008

[Thomas Hamelryck]

Dear colleagues,

The Structural Bioinformatics group at the Bioinformatics Center, University
of Copenhagen, is organizing a one-day conference on Machine Learning in
Structural Bioinformatics  on Wednesday, April
23rd 2008, at the Biocenter, Copenhagen, Denmark. Topics include
probabilistic methods for structure determination from NMR, X-ray and SAXS
data.

Registration is free for academia, and for companies that are members of
BioSys .

Hope to meet you at the conference!

Best regards,
-- 
Thomas Hamelryck
Group leader Structural Bioinformatics
Bioinformatics center
Institute of Molecular Biology
University of Copenhagen
Ole Maaloes Vej 5
DK-2200 Copenhagen N
Denmark
http://wiki.binf.ku.dk/User:Thomas_Hamelryck
http://wiki.binf.ku.dk/Protein_structure

Re: [ccp4bb] Does NCS bias a randomly-chosen test set (even if not enforced)?

[Dirk Kostrewa]

Dear Ed,

although, I don't think that a comparison of refinement in a higher  
and a lower symmetry space group is valid for general NCS cases, I  
will try to answer your question. Here are my thoughts for two  
different cases:


(1) You have data to atomic resolution with high I/sigma and low Rsym  
(I assume high redundancy). The n copies of the asymmetric unit in  
the unit cell are really identical and obey the higher symmetry (so,  
not a protein crystal). When you process the data in lower symmetry  
(say, P1), the non-averaged "higher-symmetry"-equivalent Fobs will  
differ due to measurement errors, and thus reflections in the working- 
set will differ to "higher-symmetry"-related reflections in the test- 
set due to these measurement errors. If you then refine the n copies  
against the working-set in the lower P1 symmetry, you minimize |Fobs 
(work)-Fcalc|, resulting in Fcalcs that become closer to the working- 
set Fobs. As a consequence, the Fcalcs will thus diverge somewhat  
from the test-set Fobs. However, since this atomic model is assumed  
to be very well defined obeying the higher symmetry, and,  
furthermore, the working-set contains well measured "higher-symmetry"- 
equivalent Fobs, the resulting atomic positions, and thus the Fcalcs,  
will be very close to their equivalent values in the higher-symmetry  
refinement. Therefore, the Fcalcs will also be still very similar to  
the "higher-symmetry"-equivalent Fobs in the test-set, and I would  
expect a difference between Rwork and Rfree ranging from "0" to the  
value of Rsym. In other words, the Fobs in the test-set are not  
really independent of the reflections in the working-set, and thus  
Rfree is heavily biased towards Rwork.
In this case, I would not expect large differences in the outcome due  
to the additional application of "NCS"-constraints/restraints.


(2) You have data to non-atomic lower resolution, weak I/sigma and  
poor Rsym. It is impossible to say whether the n copies of the  
asymmetric unit in the unit cell are really identical, but they are  
treated so assuming the higher symmetry (so, a real protein crystal).  
For data processing, the same holds true as for case (1). In  
contrast, here I think that it makes a difference, whether you apply  
"NCS"-constraints/restraints between the n copies in the lower  
symmetry P1, or not. If you apply "NCS"-constraints or strong "NCS"- 
restraints, the n copies are made equal and you get n times the  
average structure. This is similar to the refinement in the higher  
symmetry, except that again you minimize the discrepancy between  
Fcalcs and working-set Fobs, which will increase the discrepancy to  
the "higher-symmetry"-related Fobs in the test-set. But since the  
Fobs in the test-set are still not really independent to the Fobs in  
the working-set, I would again expect maximum differences between  
Rwork and Rfree in the same order of magnitude as Rsym. So, Rfree is  
still biased towards Rwork, but it might be more difficult to notice  
this. But if you do not apply "NCS"-constraints/restraints, you give  
the less well-defined atomic model more freedom to converge against  
the working-set Fobs, resulting in a higher discrepancy between Rwork  
and Rfree. But since the Fobs in the working set still contain  
"higher-symmetry"-equivalent Fobs, you will end up with a model that  
still shows some similarity to the refined structure in the higher  
symmetry. As a result, the Rfree is even then not really independent  
of Rwork, but it might be even more difficult to notice this,  
depending on data resolution and quality. Here, I can't give a range  
of differences between Rwork and Rfree.


So, this is still not quantitative, and I hope that I'm not  
completely wrong with my argumentation.


These lower vs. higher symmetry examples given above are only  
transferable to reality in special NCS-cases with pseudo-higher  
symmetry (what Dale Tronrud discussed). Taking these special cases  
aside, what do the NCS experts say to my original statement that  
precautions against NCS bias in Rfree must only be taken if NCS- 
constraints/restraints are really applied during refinement?


Best regards,

Dirk.

Am 08.02.2008 um 21:43 schrieb Edward A. Berry:


Clarification-

Someone wrote:
Ah- that's going way to fast for the beginners, at least one of  
them!

Can someone explain why the R-free will be very close to the R-work,
preferably in simple concrete terms like Fo, Fc, at sym-related
reflections, and the change in the Fc resulting from a step of  
refinement?


Ed

Hi Ed,
  Here's what I think they're saying:
  If the NCS is almost crystallographic, then one wedge of spots  
will be almost identical to another wedge.  If spot "a" is in the  
test set, but the almost-crystallographically identical spot "a' "  
in the 2nd wedge isn't, then because you're refining directly  
against a', spot a doesn't really count as "free".

  Was that the question?

Thanks, but

Re: [ccp4bb] microsoft 3-button wheel mouse with OS X 10.5

[Ronnie Berntsson]

Hi,

These commands does maybe not give you a full featured focus-follows- 
mouse, but it certainly makes your life easier if you work a lot in OS  
X and X11.. w


defaults write com.apple.x11 wm_ffm -bool false
defaults write com.apple.x11 wm_click_through -bool true

These two commands should to the trick and save you quite some extra  
mouse clicks.


Cheers,
Ronnie


On Jan 23, 2008, at 4:24 PM, William Scott wrote:


Yes, thanks, that does it for the Terminal.app, but not for any of the
rest.  It would be great to have such a feature globally.

mb1pja wrote:

Dear Bill

William Scott wrote


Aqua simply behaves by slightly different rules.  Although I am a
slobbering OS X fan, this lack of customizability to me, as well as
a lack
of focus-follows-mouse, it a negative.



To get focus-follows-mouse in Aqua, type the following in your
Terminal window:

defaults write com.apple.Terminal FocusFollowsMouse -string YES

and then logout and log in again or quit and restart Terminal.

I had thought I originally got that useful hint from your own  
fabulous

PX on OSX pages but clearly not.



best wishes

Pete Artymiuk



On 20 Jan 2008, at 15:39, William Scott wrote:


Hi David:

david lawson (JIC) wrote:

Dear All,

Sorry for the slightly off-topic subject.

We have recently bought a few iMacs for crystallography. I'm not
keen on
the supplied "mighty mouse"


May I have them?


so I have switched to using a microsoft
3-button wheel mouse. I would like to configure it so that it
behaves as
it would with other unix systems such as RH Linux.


You managed to use "Microsoft", "behaved" and "Linux" (albeit RH)
all in
one sentence without a hint of irony.




i.e.
(1) double-clicking with LH button on a file name selects ALL of  
the

file name, not just up to the first full stop.


Although your choice of Microsoft products shows dedication to a
company
with a firm reputation for placing the customizability needs of its
customers ahead of its own desire to make profits, the first thing  
to

realize is that you should never ever ever install their drivers.
Ever. So
if you did, take them out, now, and reboot. I'll wait.  It is still
early
Sunday morning here.


(2) clicking the scroll wheel pastes the selected text AND it can  
be

done multiple times without re-selecting.


When you've gotten rid of the drivers, this should now work. In
Apple's
Terminal program (as of 10.5) and iTerm (as of 1215), you just set  
the

preference to do middle-button-paste and left-button select, and
Blair's
your uncle. Unfortunately, in pretty much every other application I
can
think of on OS X, this, sadly, does not work, and there is nothing
Steve
Gates will let you do about it.



(2) I would like these functions to work in terminal windows, the
ccp4i
gui and web pages (and probably a few other things I haven't
thought of
yet!) AND be able to transfer the selected text between  
applications.


I'd like to be at my ideal high-school weight, be paid more than a
postdoc, and, well ...  Getting the OS X gui to play nice with X11  
is

sometimes challenging.  With the exception of Terminal and iTerm,
you have
to explicitly put stuff in the copy/paste buffer (command-C) before
it is
in the system clipboard.  Then you can paste to X11 programs with a
middle-button click, but this only works if you uninstalled that  
viral

driver. Going from X11 to aqua programs requires selecting the text
in the
usual X11 manner but explicitly issuing the paste command (command-
p).  If
you are using KDE X11 applications, you are really in for headaches.

To get whole-string selection in iTerm or Terminal, there is a
preference
setting that allows you to input which characters you want to have
considered parts of a "word" for click-to-select purposes.
Unfortunately,
pretty much every other application lacks this customizability, and
I know
of no system-wide preference setting that would enable you to do  
this

globally.

Aqua simply behaves by slightly different rules.  Although I am a
slobbering OS X fan, this lack of customizability to me, as well as
a lack
of focus-follows-mouse, it a negative.

If you really need the canonical linux behavior, you can install
gnome,
xfce4, KDE, enlightenment, or any number of other window managers  
via
fink. I've found KDE buggy and the XFCE4 is way out of date.   
Gnome is

probably the best bet, and there is a major effort now to bring it
completely up to date in fink.



I have installed the microsoft intellipoint drivers that seem to  
give

more control over configuring the various buttons through "system
preferences", but I still can't get what I want.


Therein lies the problem, I am afraid. OS X will behave better using
the
default settings.  It may be possible to tinker around with the
driver,
including separate settings in X11, to recover canonical behavior,
but for
purposes of sanity, uninstall them first, get everything working as
best
as possible, verify middle-button-paste works in X11, verify X

[ccp4bb] Best optics for Rikagu Generator....

[Karthikeyan S.]

Dear All,

Apologise for off-topic from ccp4!

We are planning to upgrade mirror optics to Confocal multi layer optics 
for our Ultrax-18 Rigaku X-ray generator along with Mar345 detector.
I want to have comparison between osmic blue confocal multi layer optics 
with xenocs FOX 2D Cu 12_38 focusing optics. Which one will be best for our

system? or Is there any better optics is there?

Suggestions are highly welcome and appreciated! You can reply to me 
direclty if you wish!


Thanking you
Sincerely
Karthik

[ccp4bb] First Announcement: 6th International NCCR Symposium on New Trends in Structural Biology, September 8 + 9, 2008

[Patrick Sticher]

Dear colleagues,

it is our pleasure to announce the 6th International NCCR Symposium 
taking place this September.



First Announcement:

6th INTERNATIONAL NCCR SYMPOSIUM ON NEW TRENDS IN STRUCTURAL BIOLOGY
September 8 + 9, 2008
Lecture Hall KOH B10, University of Zurich, Switzerland

Confirmed speakers to date:
Stephen Kowalczykowski ¦ Keiichi Namba ¦ Poul Nissen ¦ Andrej Sali ¦ A. 
Joshua Wand


www.structuralbiology.uzh.ch/symposium2008.asp

The registration slot opens end of March.
Online registration will be possible directly from the above mentioned 
web site.


The symposium will be followed directly by the Annual Meeting of the 
Swiss Society for Crystallography with two or three additional short 
lectures. Participants of the NCCR Symposium are invited to join this 
event as well.



We do hope that this conference is of interest to you and would be 
pleased to welcome you in Zurich this fall.


With best regards,
Patrick Sticher

_
Visit the NCCR on the Internet
www.structuralbiology.uzh.ch

Dr. Patrick Sticher Moser
NCCR Scientific Officer
Institute of Biochemistry
University of Zürich
Winterthurerstrasse 190
CH - 8057 Zürich

Phone+41 / (0)44 / 635 54 84
Fax+41 / (0)44 / 635 59 08
Mail[EMAIL PROTECTED]