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On the possibility of using polycrystalline material in the development of structure-based generic assays

Journal Article · · Acta Crystallographica. Section D: Biological Crystallography
 [1];  [2];  [3];  [4];  [5]
  1. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source; DOE/OSTI
  2. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
  3. Stony Brook Univ., NY (United States). Dept. of Physics and Astronomy
  4. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source; Stony Brook Univ., NY (United States). Dept. of Biomedical Engineering
  5. Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source; Stony Brook Univ., NY (United States). Dept. of Physics and Astronomy
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 stereo-chemically restrained Rietveld refinement.
Research Organization:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division
Grant/Contract Number:
AC02-98CH10886
OSTI ID:
1625659
Alternate ID(s):
OSTI ID: 22347976
Journal Information:
Acta Crystallographica. Section D: Biological Crystallography, Journal Name: Acta Crystallographica. Section D: Biological Crystallography Journal Issue: 4 Vol. 65; ISSN ABCRE6; ISSN 0907-4449
Publisher:
International Union of CrystallographyCopyright Statement
Country of Publication:
United States
Language:
English

Cited By (1)

Acoustic methods for high-throughput protein crystal mounting at next-generation macromolecular crystallographic beamlines journal August 2013

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