On the possibility of using polycrystalline material in the development of structure-based generic assays
Journal Article
·
· Acta Crystallographica. Section D: Biological Crystallography
- National Synchrotron Light Source, Brookhaven National Laboratory, Upton, NY 11973-5000 (United States)
- Department of Physics and Astronomy, Stony Brook University, Stony Brook, NY 11794-3800 (United States)
The correlation coefficients calculated between raw powder diffraction profiles can be used to identify ligand-bound/unbound states of lysozyme. The discovery of ligands that bind specifically to a targeted protein benefits from the development of generic assays for high-throughput screening of a library of chemicals. Protein powder diffraction (PPD) has been proposed as a potential method for use as a structure-based assay for high-throughput screening applications. Building on this effort, powder samples of bound/unbound states of soluble hen-egg white lysozyme precipitated with sodium chloride were compared. The correlation coefficients calculated between the raw diffraction profiles were consistent with the known binding properties of the ligands and suggested that the PPD approach can be used even prior to a full description using stereochemically restrained Rietveld refinement.
- OSTI ID:
- 22347976
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Journal Name: Acta Crystallographica. Section D: Biological Crystallography Journal Issue: Pt 4 Vol. 65; ISSN ABCRE6; ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
Acoustic methods for high-throughput protein crystal mounting at next-generation macromolecular crystallographic beamlines
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journal | August 2013 |
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