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| General Section People Events Program Details |
Predoctoral Trainee
X-ray crystallography is the most direct and commonly used technique for obtaining atomic resolution information on the three-dimensional structure of biological macromolecules. However, acquiring a fully mechanistic understanding of how a protein’s structure leads to its function requires knowledge not only of the static arrangement of its atoms, but of its inherent flexibility and dynamic properties as well. While raw X-ray diffraction data does contain information on protein dynamics, conventional crystallographic models typically underutilize or even misrepresent this information. My current research investigates the ability of an alternate approach to modeling crystal structures known as ensemble refinement to extract more accurate measurements of protein motion from X-ray diffraction data. Our results suggest that ensemble refinement can more accurately describe the magnitude and distribution of deviations from the average structure, and improves the general agreement between the model and the experimental X-ray data. CVE. Levin's CV (.pdf format) PublicationsSearch for publications by Elena Levin(Pub Med) |
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