Re: [ccp4bb] Is it possible to fix the position of an atom during real space fitting in Coot?

[Paul Emsley]

On 13/03/2018 20:12, Ana Luísa Moreira de Carvalho wrote:
You can find the tool “Fixed Atoms” in the Refinement Toolbar (the side menu). Just click Fix Atom and then 
click the atom(s) you wish to fix. It won’t move in real space refinement or in regularisation.



That's right, Ana Luísa.

And for the record, it's often useful to move fixed atoms. Use Ctrl Left-mouse click and drag. So Fixed 
Atoms move when nothing else moves and stay still when everything else refines. Paradoxical maybe, but 
useful. I use it when I have to assert my authority over recalcitrant atoms.


Paul.

Re: [ccp4bb] How to get Imean/SIGImean from separated anomalous data?

[Edward A. Berry]

Thanks- that works!
pdb-redo/tools/cif2cif in.cif out.cif
eab


On 03/13/2018 05:47 PM, Robbie Joosten wrote:

Hi Ed,

The pdb-redo program cif2cif does that. I implemented this feature because 
there was no obvious CCP4 program that did this. You have to have your data in 
mmCIF format though.

Cheers,

Robbie

Sent from my Windows 10 phone

--
*From:* CCP4 bulletin board  on behalf of Edward A. Berry 

*Sent:* Tuesday, March 13, 2018 10:25:25 PM
*To:* CCP4BB@JISCMAIL.AC.UK
*Subject:* [ccp4bb] How to get Imean/SIGImean from separated anomalous data?
I want to work with an mmcif file that has I+,sigI+,I-,SigI-;
   in different columns for each reflection (no Imean).
cif2mtz gives those same columns in the output mtz, with or without ANOMALOUS 
keyword.
cif2mtz and truncate seem to need the anomalous data as separate reflections 
hkl and -h-k-l in order to calculate Imean or Fmean. What is the best way to do 
this?
Thanks,
eab

[ccp4bb] release of SPHIRE 1.0

[Stefan Raunser]

Dear colleagues,
We are excited to announce the release of the latest version of our SPHIRE 
software suite (SPHIRE 1.0) (co-distributed with EMAN 2.21), which is now 
available from our website:

http://sphire.mpg.de

Main new components and updates:

- SORT3D – A novel 3D sorting program based on novel concepts of 
reproducibility. We tested it on several high-resolution projects in our lab 
and were able to gain valuable and unparalleled insight into data heterogeneity.

- MERIDIEN – Rapid ML 3D refinement. We have introduced initialization of the 
program directly from 3D orientation parameters, as opposed to standard mode, 
which is initiated by an initial template structure. The new mode allows the 
user to rapidly perform local refinements of data subsets obtained with SORT3D. 
The two programs, MERIDIEN and SORT3D, thus serve as a perfect tool for 
exploration of data set heterogeneity.

- We have streamlined the processing workflow and the GUI interface 
facilitating users’ interactions with the system.
- The new release is accompanied by extensive documentation including tutorials 
explaining the underlying concepts.

For any issues and inquiries, the SPHIRE team is accessible 24/7 via the 
mailing list. We sincerely hope that the updated SPHIRE 1.0 will meet your 
expectations and be a helpful advance in high-resolution cryo-EM.

Your SPHIRE development team

Toshio, Markus, Felipe, Thorsten, Christos, and Stefan – MPI Dortmund

Zhong and Pawel - UTH Texas

(Follow us on Twitter: 
https://twitter.com/SPHIRE_Package)
-
Stefan Raunser, Ph.D.

Director, Department of Structural Biochemistry
Max Planck Institute of Molecular Physiology
Otto-Hahn-Str. 11
44227 Dortmund, Germany
tel: +49-231-133-2300

and

Adjunct Professor, Faculty of Chemistry and Chemical Biology
Technical University Dortmund

Honorary Professor, Centre for Medical Biotechnology, Faculty of Biology
University Duisburg-Essen

[ccp4bb] release of SPHIRE 1.0

[Stefan Raunser]

Dear colleagues,
We are excited to announce the release of the latest version of our SPHIRE 
software suite (SPHIRE 1.0) (co-distributed with EMAN 2.21), which is now 
available from our website:

http://sphire.mpg.de

Main new components and updates:

- SORT3D – A novel 3D sorting program based on novel concepts of 
reproducibility. We tested it on several high-resolution projects in our lab 
and were able to gain valuable and unparalleled insight into data heterogeneity.

- MERIDIEN – Rapid ML 3D refinement. We have introduced initialization of the 
program directly from 3D orientation parameters, as opposed to standard mode, 
which is initiated by an initial template structure. The new mode allows the 
user to rapidly perform local refinements of data subsets obtained with SORT3D. 
The two programs, MERIDIEN and SORT3D, thus serve as a perfect tool for 
exploration of data set heterogeneity.

- We have streamlined the processing workflow and the GUI interface 
facilitating users’ interactions with the system.
- The new release is accompanied by extensive documentation including tutorials 
explaining the underlying concepts.

For any issues and inquiries, the SPHIRE team is accessible 24/7 via the 
mailing list. We sincerely hope that the updated SPHIRE 1.0 will meet your 
expectations and be a helpful advance in high-resolution cryo-EM.

Your SPHIRE development team

Toshio, Markus, Felipe, Thorsten, Christos, and Stefan – MPI Dortmund

Zhong and Pawel - UTH Texas

(Follow us on Twitter: 
https://twitter.com/SPHIRE_Package)
-
Stefan Raunser, Ph.D.

Director, Department of Structural Biochemistry
Max Planck Institute of Molecular Physiology
Otto-Hahn-Str. 11
44227 Dortmund, Germany
tel: +49-231-133-2300

and

Adjunct Professor, Faculty of Chemistry and Chemical Biology
Technical University Dortmund

Honorary Professor, Centre for Medical Biotechnology, Faculty of Biology
University Duisburg-Essen

[ccp4bb] How to get Imean/SIGImean from separated anomalous data?

[Edward A. Berry]

I want to work with an mmcif file that has I+,sigI+,I-,SigI-;
 in different columns for each reflection (no Imean).
cif2mtz gives those same columns in the output mtz, with or without ANOMALOUS 
keyword.
cif2mtz and truncate seem to need the anomalous data as separate reflections 
hkl and -h-k-l in order to calculate Imean or Fmean. What is the best way to do 
this?
Thanks,
eab

Re: [ccp4bb] Is it possible to fix the position of an atom during real space fitting in Coot?

[Ana Luísa Moreira de Carvalho]

You can find the tool “Fixed Atoms” in the Refinement Toolbar (the side menu). 
Just click Fix Atom and then click the atom(s) you wish to fix. It won’t move 
in real space refinement or in regularisation.
Cheers!

> On 13 Mar 2018, at 19:46, Steve Chou  wrote:
> 
> Dear Coot developers and CCP4 list subscribers,
> 
> The density of my map is not perfect. However, I know where a specific atom 
> should be located. Every time I did real space fitting, the atom and the 
> associated chemical groups in the whole ligand ran away. Is there a way to 
> fix the position of this atom, and let the force field drive the fitting of 
> the rest of the atoms in the ligand?
> Many thanks in advance!
> Steve
> 
> -- 
> Steve Chou
> 
> 

Research Assistant Professor at UCIBIO@REQUIMTE-FCT-NOVA
***
Biologia Estrutural - Cristalografia de Raios-X (Gab 6.34)
Dep. Quimica, FCT-UNL
2829-516 Caparica
Portugal
Phone: 00351212948300 (ext: Gab: 10940; Lab: 10962; X-ray Lab: 10915)
Fax: 00351212948550
http://docentes.fct.unl.pt/almc 
http://sites.fct.unl.pt/xtal 
https://orcid.org/-0002-3824-0240/print
***

Re: [ccp4bb] Is it possible to fix the position of an atom during real space fitting in Coot?

[Eleanor Dodson]

Yes - you can "FixAtom"  - I cant remember which menu it is under - real
space rene I think.. Will check tomorrow

Eleanor

On 13 March 2018 at 19:46, Steve Chou  wrote:

> Dear Coot developers and CCP4 list subscribers,
>
> The density of my map is not perfect. However, I know where a specific
> atom should be located. Every time I did real space fitting, the atom and
> the associated chemical groups in the whole ligand ran away. Is there a way
> to fix the position of this atom, and let the force field drive the fitting
> of the rest of the atoms in the ligand?
> Many thanks in advance!
> Steve
>
> --
> Steve Chou
>
>
>

[ccp4bb] Is it possible to fix the position of an atom during real space fitting in Coot?

[Steve Chou]

Dear Coot developers and CCP4 list subscribers,

The density of my map is not perfect. However, I know where a specific atom
should be located. Every time I did real space fitting, the atom and the
associated chemical groups in the whole ligand ran away. Is there a way to
fix the position of this atom, and let the force field drive the fitting of
the rest of the atoms in the ligand?
Many thanks in advance!
Steve

-- 
Steve Chou

[ccp4bb] University of Oxford - Structural Biology Postdoc position with focus on Drug Discovery - DEADLINE 16/03/18!

[Kilian Huber]

The Huber lab at the Structural Genomics Consortium (SGC)/Target Discovery 
Institute is looking for a highly motivated and enthusiastic postdoctoral 
fellow to join our team to explore the structure and function of human proteins 
linked to cancer and inflammatory diseases. Our group is focused on chromatin 
regulation, ATPases, and ubiquitin signalling. The position is funded through 
an EU-IMI grant and presents an exciting opportunity to study unexplored human 
proteins and develop small molecule tool compounds in collaboration with an 
interdisciplinary team of scientists from both academia and big pharma. 
Applicants are expected to have a strong and demonstrable track record of 
protein biochemistry and x-ray crystallography; experience with cryoEM is a 
plus but not a requirement.

https://www.recruit.ox.ac.uk/pls/hrisliverecruit/erq_jobspec_details_form.jobspec?p_id=133660

Deadline for applications: 12.00 noon on Friday 16 March 2018

[ccp4bb] Mosaicity histogram in HKL 3000R

[Annette Herta Erbse]

Hi Everyone,


I am seeing something strange with HKL 3000R with regard to the mosaicity 
histogram and was wondering if anyone has come across something like it before. 
From the HKL 2000 manual  I understand that the mosaicity histogram should to 
go through 0 close to 0.5 partiality, to have higher values in the negative 
zone and to go down to close to 0 at +mosaicity/2. I am  working on a Rigaku 
system (XtaLAB MM003 , AFC11 Partial-χ 4-axis goniometer , PILATUS 200K 
detector) and it came with HKL 3000R. I have looked at quite a few different 
crystals from Lysozyme to RNA and in every case the first zone in the histogram 
is the 0 zone and it is (somewhat) close to  0.5 partiality and the histogram 
goes down from there to close to 0 at + mosaicity/2. But the histogram has 
nothing in negative zones. I am trying to understand how that can be and if 
this indicates a problem of some kind. Or maybe I am simply doing something 
stupid wrong? I am using a 3D window that covers about twice the mosaicity. I 
have seen it with data that were collected with 0.25,  0.5 or 1 degree 
oscillation.  I appreciate any advice.

Thanks - Annette

Annette H. Erbse
Department of Chemistry & Biochemistry
University of Colorado at Boulder

Voice: ++1-303-492-0528 (office)
Fax: ++1-303-492-8425
Email:  er...@colorado.edu
Office: JSCB C316

[ccp4bb] New SHELX versions and email address

[George Sheldrick]

Here is another attempt from my old email address. I was not registered 
to use the email lists from my

new address, but please use it in future!

New versions of SHELXE, SHELXL and SHELXT and also Anna Luebben's 
program pdb2ins that provides
a quick way of setting up a shelxl refinement given a PDB code may now 
be downloaded via the SHELX
homepage at *shelx.uni-goettingen.de*  Details of the changes may be 
found under 'recent changes' on
the homepage. The old shelx download site has not been updated and will 
be decommissioned soon, it is
on a very old computer that is on its last legs and is subject to power 
outages caused by building work.


*Please also note my new email address gsheldr (at) uni-goettingen.de !*

George

--
Prof. George M. Sheldrick FRS
Dept. Structural Chemistry,
University of Goettingen,
Tammannstr. 4,
D37077 Goettingen, Germany
Tel. +49-551-39-33021 or +49-5594-227312

[ccp4bb] PhD positions in structural biology at EMBL Grenoble

[Kowalinski Eva]

Dear colleagues,

I would like to inform you about the ongoing call for applications to the EMBL 
International PhD programme. In particular, I would like to draw your attention 
to several open PhD positions in the area of structural biology at EMBL 
Grenoble.

The EMBL international PhD programme promotes excellence in basic molecular 
life sciences research throughout Europe and currently hosts approximately 230 
PhD students from around 50 countries. The programme is committed to providing 
EMBL PhD students with the best starting platform for a successful career in 
science.

We welcome applications from highly qualified students of all nationalities 
with background in Biology, Chemistry, Physics, Mathematics, Computer Science, 
Engineering and Molecular Medicine. Our students have an outstanding 
publication record, are a vital part of our global collaborations and receive 
their degrees jointly with our network of excellent partner universities in 17 
different countries. Our PhD positions come with generous fellowships, 
including broad health care benefits and pension access. 

The registration deadline is 02 April 2018.
The deadline for submission of the online application is 09 April 2018.
Interviews will take place in the beginning of July 2018.

For more information and application, please visit 
https://www.embl.fr/training/eipp/index.html or contact the Graduate Office at 
pred...@embl.de.

Please feel free to share this message with potential candidates.



Dr. Eva Kowalinski
Group Leader

EMBL Grenoble,71 Avenue des Martyrs, 38042 Grenoble Cedex 09, France

T +33 476 20 74 46

Re: [ccp4bb] Strange Diffraction pattern! Protein/DNA complex or DNA alone crystal?

[Philippe BENAS]

Dear Joseph,
I fully agree with Daniel Himmel's answer but you might be able to "index" your 
reflections and get a approximate cell parameters.
I did that in the past with crystals that diffracted very poorly up to 15 
angst. I used HKL200 at that time, cheated with the distance (HKL2000 won't 
accept indexing with too low resolution spots) and selected individual spots 
manually.It was enough for making Matthews analysis for each putative space 
group.The complex formation between the protein and the RNA was confirmed by a 
stoechiometric amount of each macromolecule resulting from OD spectra 
deconvolution taken on dissolved crystals, using a spectrum for the protein 
alone and a spectrum for the RNA alone as references.
Best regards,
Philippe Philippe BENAS, Ph.D.

Laboratoire de Cristallographie et RMN Biologiques, UMR 8015 CNRS
Faculté de Pharmacie, Université Paris Descartes
Case 48
Av, de l'Observatoire
F-75270 PARIS cedex 06
+33.1.5373.1599
E-mails: philippe.be...@parisdescartes.fr, philippe_be...@yahoo.fr
URLs: http://lcrbw.pharmacie.univ-paris5.fr/ , 
http://lcrbw.pharmacie.univ-paris5.fr/spip.php?article18



  De : Joseph Ho 
 À : CCP4BB@JISCMAIL.AC.UK 
 Envoyé le : Lundi 12 mars 2018 12h54
 Objet : [ccp4bb] Strange Diffraction pattern! Protein/DNA complex or DNA alone 
crystal?
   
Dear all:


I would like to seek your wisdom on our latest diffraction pattern. We
have been working on protein/DNA complex. The protein and DNA have
similar MW. By binding assay, we know the minimal length of DNA. (The
Kd is 0.1-1 microMolar and we can see the complex formation in size
exclusion chromatography up to 200mM NaCl but also some unbound form)
After trying different length of DNA, we recently obtained many
crystal hits (the percipient is either PEG400 or MPD). The final ratio
(prior to protein crystallization) between protein and DNA is 1:1.6
considering some loss of protein during concentration. The crystal is
birefringent. Since high conc. of PEG400 (MPD), the crystals were
directly frozen in liquid N2. However, crystals only diffract to 8-10
angstrom (anisotropic) and also  weird striking line are present
(please see attachment). Do you think if it is  DNA alone crystal or
protein/DNA complex crystal?
How should I improve the diffraction quality?



PS. We have done some tests. For example, set up the same conditions
with DNA alone. I also tried to dissolve crystals in Bradford assay
solution and I believe I saw some blueish color. But none of these
tests are conclusive.

Thanks for your suggestion.

Joseph


   

[ccp4bb] Joint Liverpool/Diamond PhD studentship

[Rigden, Dan]

Dear all,

A fully-funded 4-year PhD studentship, joint between the University of 
Liverpool and the Diamond Light Source, is now available. Paying an enhanced 
stipend, it involves application of computational methods to characterise and 
solve diffraction datasets from crystals of transmembrane helical proteins. The 
studentship is based at both Liverpool and Diamond Light Source providing a 
unique opportunity to develop and apply computational methods at world leading 
X-ray facilities. The closing date for applications is Friday 6th April. 
Applicants should have or expect to graduate with a 1st or high 2:1 degree.

For details of the project and information on how to apply please see
https://www.findaphd.com/search/ProjectDetails.aspx?PJID=96121
[https://www.findaphd.com/images/logo-square-200px.png]

New computational approaches to characterise and solve multi-crystal 
diffraction datasets of transmembrane proteins from the VMXm beamline at 
University of Liverpool on 
FindAPhD.com
www.findaphd.com
PhD Project - New computational approaches to characterise and solve 
multi-crystal diffraction datasets of transmembrane proteins from the VMXm 
beamline at University of Liverpool, listed on FindAPhD.com



Daniel Rigden

[ccp4bb] Postdoctoral Research Fellow vacancy - protein kinases in Bayliss lab, Leeds

[Richard Bayliss]

I am looking for a Postdoctoral Research Fellow to explore the regulation of 
protein kinases and to contribute structural insights to drug discovery 
projects. The catalytic activities of protein kinases are controlled through 
protein-protein interactions and post-translational modifications. The project 
aims to resolve the structural basis of these mechanisms using a combination of 
protein crystallography, biochemistry, computational biology and biophysical 
approaches. The insights gleaned from these studies will underpin the 
development of allosteric kinase inhibitors.

The post is funded by a Programme Award from Cancer Research UK, and is 
available until 28 February 2020 in the first instance, renewable for a further 
2 years

Informal enquiries welcome - follow the link to apply

https://jobs.leeds.ac.uk/vacancy.aspx?ref=FBSMB1132



===
Prof. Richard Bayliss
Head of the School of Molecular and Cellular Biology
Professor of Molecular Medicine
Faculty of Biological Sciences
Astbury Building
University of Leeds
Leeds LS2 9JT

Email: r.w.bayl...@leeds.ac.uk
Tel: 0113 3439919
Twitter: @baylisslab



[cid:4AACB59B-0660-4C7C-B997-79F621AF1292]

Re: [ccp4bb] AW: [ccp4bb] Small molecule not refined in coot.

[Paul Emsley]

On 13/03/2018 07:36, M T wrote:

So finally the solution was easy access...

Thanks to someone who suggest me to do that, I created a new user, to verify if coot was ok under that 
session, and it was fine.

Then I went back on my session, I removed the files below:
0-coot-history.py
0-coot-history.scm
0-coot.state.py 
0-coot.state.scm

I restarted Coot, and loaded my files (.pdb, .mtz and .cif), Coot didn't crash and I am now able to do a 
real space refinement.


It should be my first intention to remove Coot preferences.

Regards.

2018-03-12 21:39 GMT+01:00 Paul Emsley >:


On 12/03/18 14:05, M T wrote:
> Dear all,
>
> I restart this topic because the problem was finally not solved...

You give me an opportunity to comment, I had previously missed the boat
while traveling.

>
> Summary:
> - I am working on a structure with an unnatural ligand and I want to
 > refine this ligand using Coot.

Sounds like a fine plan.

> - Each time I try to import the .cif of my ligand produced by PRODRG
> web server or through CCP4/ProDrg, coot crashes with error message
> below (see quoted messages).

The first thing to do, when Coot crashes is to check for a new revision.
There's a good chance that the problem has been fixed and is just
waiting for you to download it.

> - I sent my files to someone else and they are working on his computer
> (both are Mac and are using CCP4/Coot on same SBGRID server, with same
> files, and macOS was different).
> - I saw that my macOS was outdated (Starting SBGRID saying "- MacOS X
> versions 10.10 (Yosemite) and earlier are no longer officially
> supported").
> - I did an update of my macOS to High Sierra (10.13.3).
> - I retried with same files, Coot crashed.

For the record, the crash log would be highly helpful.

> - I went back to PRODRG server to generate a simple .cif
> (CH3-CH2-CH2-CH3).

Fine as it was in its day, PRODRG is no longer what we use for ligands.
We use Acedrg.  If you want to use SMILES, you can use it on the command
line (that's what I do). If you want to use it from a sketch, use the
Ligand Builder in Coot. You can also use pyrogen (I do).

> - I started Coot, opened the .cif file using "Import CIF
> dictionary...", Coot crashed.
>
> It seems that opening any .cif file on my computer causes Coot crash.

Edit -> Preferences -> File Selector -> Modern File Chooser

For the record (again) this is the site that I use to download Coot mac
binaries:

http://scottlab.ucsc.edu/xtal/wiki/index.php/Stand-Alone_Coot


>
>
> Anybody has an idea to solve the problem?

It was discussed on the mailing list in January and fixed by the next day.

https://www.jiscmail.ac.uk/cgi-bin/webadmin?A2=ind1801=COOT===5852


Regards,

Paul.




In case it was not clear how Michel's answer was related to mine, the reason coot was fine when starting 
from fresh is that the default option for the file selectors/choosers is "Modern" and Michel had changed 
those to "Classic" - those options get stored in $HOME/.coot-preferences. You can additionally modify them 
in your 0-coot.state.py and 0-coot.state.scm files (in the current directory).


Regards,

Paul.

Re: [ccp4bb] AW: [ccp4bb] Small molecule not refined in coot.

[M T]

So finally the solution was easy access...

Thanks to someone who suggest me to do that, I created a new user, to
verify if coot was ok under that session, and it was fine.
Then I went back on my session, I removed the files below:
0-coot-history.py
0-coot-history.scm
0-coot.state.py
0-coot.state.scm

I restarted Coot, and loaded my files (.pdb, .mtz and .cif), Coot didn't
crash and I am now able to do a real space refinement.

It should be my first intention to remove Coot preferences.

Regards.

2018-03-12 21:39 GMT+01:00 Paul Emsley :

>
> On 12/03/18 14:05, M T wrote:
> > Dear all,
> >
> > I restart this topic because the problem was finally not solved...
>
> You give me an opportunity to comment, I had previously missed the boat
> while traveling.
>
> >
> > Summary:
> > - I am working on a structure with an unnatural ligand and I want to
> > refine this ligand using Coot.
>
> Sounds like a fine plan.
>
> > - Each time I try to import the .cif of my ligand produced by PRODRG
> > web server or through CCP4/ProDrg, coot crashes with error message
> > below (see quoted messages).
>
> The first thing to do, when Coot crashes is to check for a new revision.
> There's a good chance that the problem has been fixed and is just
> waiting for you to download it.
>
> > - I sent my files to someone else and they are working on his computer
> > (both are Mac and are using CCP4/Coot on same SBGRID server, with same
> > files, and macOS was different).
> > - I saw that my macOS was outdated (Starting SBGRID saying "- MacOS X
> > versions 10.10 (Yosemite) and earlier are no longer officially
> > supported").
> > - I did an update of my macOS to High Sierra (10.13.3).
> > - I retried with same files, Coot crashed.
>
> For the record, the crash log would be highly helpful.
>
> > - I went back to PRODRG server to generate a simple .cif
> > (CH3-CH2-CH2-CH3).
>
> Fine as it was in its day, PRODRG is no longer what we use for ligands.
> We use Acedrg.  If you want to use SMILES, you can use it on the command
> line (that's what I do). If you want to use it from a sketch, use the
> Ligand Builder in Coot. You can also use pyrogen (I do).
>
> > - I started Coot, opened the .cif file using "Import CIF
> > dictionary...", Coot crashed.
> >
> > It seems that opening any .cif file on my computer causes Coot crash.
>
> Edit -> Preferences -> File Selector -> Modern File Chooser
>
> For the record (again) this is the site that I use to download Coot mac
> binaries:
>
> http://scottlab.ucsc.edu/xtal/wiki/index.php/Stand-Alone_Coot
>
> >
> >
> > Anybody has an idea to solve the problem?
>
> It was discussed on the mailing list in January and fixed by the next day.
>
> https://www.jiscmail.ac.uk/cgi-bin/webadmin?A2=ind1801=COOT===5852
>
> Regards,
>
> Paul.
>
>

[ccp4bb] Vacancies@EMBL Hamburg Unit

[Margret Fischer]

Dear all,

I would like to draw your attention to the following vacancy 
notices@EMBL Hamburg:


*Scientific Technical Officer* - Platform for Integrated Structural 
Biology at EMBL/CSSB

http://s.embl.org/HH00138

*Postdoctoral Fellowship* - Integrated Structural Biology of Peroxisomal 
Translocon Complexes

http://s.embl.org/HH00134

*Postdoctoral Fellowship* - Integrated Structural Biology of Proteins 
involved in Cancer Metastasis

http://s.embl.org/HH00132

*Postdoctoral Fellowship* - Integrated Structural Biology of the Von 
Willebrand Factor

http://s.embl.org/HH00135

*Postdoctoral Fellowship * - Integrated Structural Biology of type VII 
secretion systems

http://s.embl.org/HH00136

*Postdoctoral Fellowship* - Mechanism of nitrogen incorporation 
in multifunctional protein complexes by time-resolved structural biology

http://s.embl.org/HH00133


The deadline for all applications is April 15*. *Any inquiries can be 
sent directly to : matthias.wilma...@embl-hamburg.de 



best,
Margret
--

Margret Fischer
European Molecular Biology Laboratory
Senior Administrative Officer
Notkestrasse 85
22607 Hamburg
Germany
Tel: +49 40 89902110
Mob: +49 1754105760