Development of Procedures for Increasing the Information Content of the Biomolecular Solution X-ray Scattering Data and Improving the Accuracy of their Structural Interpretation
RAP opportunity at National Institute of Standards and Technology NIST
Development of Procedures for Increasing the Information Content of the Biomolecular Solution X-ray Scattering Data and Improving the Accuracy of their Structural Interpretation
Location
Material Measurement Laboratory, Biomolecular Measurement Division
opportunity location
50.64.51.B8254 Gaithersburg, MD
NIST only participates in the February and August reviews.
Advisers
name email phone
Alexander V. Grishaev [email protected] 240.314.6892
Description
Scattering of X-ray radiation in solution (SAXS) has a potential to become an important component in structural studies of bio-macromolecules. The main reason for its attractiveness lies in the possibility of using these data to quickly distinguish between diverse candidate structural models representing the conformation of macromolecule in solution. In this project we aim to increase the information content of the solution scattering data using approaches, such as selective labeling and contrast variation. Our second goal is to improve the accuracy with which solution scattering data of proteins and oligonucleotides can be predicted from the atomic coordinates by developing detailed models that describe the structure of the solvation layer surrounding the macromolecule based the SAXS, anomalous X-ray scattering, and neutron contrast variation measurements.
References
Grishaev A, Anthis N, Clore GM: Contrast-matched small angle X-ray scattering from a heavy atom-labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex. Journal of the American Chemical Society 134: 14686-14689, 2012
Grishaev A, Guo L, Irving T, Bax A: Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling. Journal of the American Chemical Society 132: 15484-15486, 2010
key words
Protein and RNA structure; Macromolecular solvation; X-ray and neutron scattering; Structural biology;
Eligibility
Citizenship: Open to U.S. citizens
Level: Open to Postdoctoral applicants
Stipend
Base Stipend Travel Allotment Supplementation
$82,764.00 $3,000.00
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