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[ccp4bb] Postdoctoral Fellow position

- Protein crystallography

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CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999
Previous message:
Subject: shelx HKLF4 to mtz conversion?
From: Leonard Thomas thomasle {- at -} ITS {- dot -} CALTECH {- dot -} EDU
Date: 2007-07-10
Next message:
Subject: Re: shelx HKLF4 to mtz conversion?
From: Tim Grune tim {- dot -} grune {- at -} SYNCHROTRON {- dot -} VIC {- dot -} GOV {- dot -} AU
Date: 2007-07-10


Subject: Postdoctoral Fellow position
From: Stewart Turley turley {- at -} U {- dot -} WASHINGTON {- dot -} EDU
Date: 2007-07-10

This notification is posted on behalf of Prof Wim Hol. Interested parties should reply to him at:

wghol@u.washington.edu

or at the address below.


Postdoctoral Fellow – Structural Biology of the RNA editing editosome

JOB DESCRIPTION:
The project aims at understanding the structure and functioning of the unique RNA-editing “editosome “ from Trypanosoma brucei and related trypanosomatid protozoan species. These organisms are the causative agents of a variety of diseases in tropical and subtropical areas, including sleeping sickness in Sub-Saharan Africa, Chagas’ disease in Latin America and leishmaniasis throughout the tropics and subtropics. Several essential genes in the mitochondria of these protozoa undergo a fascinating U-insertion/deletion RNA editing process involving several protein and multi-protein complexes. The RNA-editing editosome of about 1.5 million Daltons performs the actual editing steps, involving an enzyme-cascade principle. The editosome consists of over 15 different proteins with most, if not all, of these proteins present in multiple copies.

The goal of the project is to unravel, by molecular biology and crystallographic approaches: (i) protein-protein and protein-RNA interactions within the editosome; and, (ii) crystal structures of components and sub-complexes of this multi-protein assembly in complex with a variety of RNA molecules. Since several of the editosome proteins have been shown to be essential for the parasites, the results obtained provide a platform for structure-based drug design.

The successful candidate will have the opportunity to carry out (i) molecular biology, protein expression and purification methods to obtain insight into protein-protein and protein-RNA interactions involving the editosome, and (ii) to determine high resolution crystal structures of individual editosome components, and in particular of large sub-complexes of the editosome with RNA. Numerous expression systems are already available for preparing complexes containing multiple editosome proteins.

For further information regarding the editosome see:
Deng, J., Schnaufer, A., Salavati, R., Stuart, K. & Hol, W. G. J. (2004). High Resolution Crystal Structure of an Editosome Enzyme from Trypanosoma brucei: RNA Editing ligase I. J Mol Biol 343, 601-613

Deng, J., Lewis Ernst, N., Turley, S., Stuart, K. & Hol, W. G. J. (2005). Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. EMBO J. 24, 4007-4017.

For information regarding the research in our lab see the websites:
http://www.bmsc.washington.edu/WimHol/
and
http://depts.washington.edu/biowww/faculty/hol.html

JOB REQUIREMENTS:
- Good knowledge and extensive experience with molecular biology for protein overexpression
- Experience with:
- protein expression and purification methods of soluble proteins in E coli
- characterizing purified soluble proteins
- crystallization methods for proteins
- protein crystal cryo-protection procedures
- protein structure determination methods, including: X-ray diffraction data collection and data processing; selenomethionine SAD and MAD phasing and/or multiple isomorphous replacement and/or molecular replacement; density modification; model building; crystallographic refinement; structure analysis and structure validation procedures using multiple computer programs and interactive graphics techniques.

- Excellent interpersonal skills to function optimally in the editosome project team and to cooperate with collaborators in other institutions.

The Following experience would be a plus:
- Molecular biology for obtaining truncated protein variants and implementing surface mutations to enhance the probability of crystal growth
- production of RNA
- protein expression and purification methods of soluble proteins in insect cells


START DATE: Immediately

INSTITUTION: Department of Biochemistry
Biomolecular Structure Center
School of Medicine
Box 357742
University of Washington
Seattle, WA, 98195 USA

CCP4bb navigation

CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999
Previous message:
Subject: shelx HKLF4 to mtz conversion?
From: Leonard Thomas thomasle {- at -} ITS {- dot -} CALTECH {- dot -} EDU
Date: 2007-07-10
Next message:
Subject: Re: shelx HKLF4 to mtz conversion?
From: Tim Grune tim {- dot -} grune {- at -} SYNCHROTRON {- dot -} VIC {- dot -} GOV {- dot -} AU
Date: 2007-07-10



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