[phenixbb] post-doc position at SSRL

van den Bedem, Henry vdbedem at slac.stanford.edu
Mon Oct 17 15:02:00 PDT 2011

Modeling Conformational Ensembles of Proteins and Complexes

A post-doctoral position with a focus on modeling conformational ensembles of proteins and complexes is available immediately in the Structural Genomics Division of Stanford Synchrotron Radiation Lightsource at the SLAC National Accelerator Laboratory (http://ssrl.slac.stanford.edu).

Macromolecules and assemblies are studied by a variety of experimental techniques, including protein crystallography and Small Angle X-ray Scattering. Nano-crystallography and single particle imaging data from the Linac Coherent Light Source (LCLS), a first-of-its-kind free electron laser, are also being targeted at these systems. Accurately modeling the conformational variability of macromolecules is essential to understanding their cellular function.

This position at the forefront of computational structural biology aims to develop advanced algorithms to fit domains or proteins to experimental data from multiple sources while allowing for significant conformational changes. The goal is to automatically compute 3-D models, and to provide structural insights into functionally relevant dynamics, especially for time-resolved experiments or a series of static structures. The position offers the opportunity to closely collaborate with the Stanford Computer Science Department and work with X-ray, SAXS and LCLS nanocrystallography data. SLAC houses ample computational resources. Funding is available for up to 3 years. The starting date is as soon as possible.

Candidates should have a recent PhD in computer science, applied mathematics, computational biology/crystallography or a related field with strong programming skills. Please send a CV, a short summary of your research experience and two letters of recommendation to Henry van den Bedem (vdbedem at slac.stanford.edu). Further details are available upon request.

Relevant publications:

Yao et al. Sampling-based exploration of folded state of a protein under kinematic and geometric constraints. Proteins: Structure, Function, and Bioinformatics (in press).

Fraser et al. (2011) Accessing protein conformational ensembles using room-temperature X-ray crystallography. PNAS 108:16247-16252

van den Bedem et al. (2009) Modeling discrete heterogeneity in X-ray diffraction data by fitting
multi-conformers. Acta Cryst. D65:1107-1117

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