On the possibility of using polycrystalline material in the development of structure-based generic assays.
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.
Allaire
Marc
M
National Synchrotron Light Source, Brookhaven National Laboratory, Upton, NY 11973-5000, USA. allaire@bnl.gov
Moiseeva
Natalia
N
Botez
Cristian E
CE
Engel
Matthew A
MA
Stephens
Peter W
PW
D000117:Acetylglucosamine / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002645:Chickens; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D005947:Glucose / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D009113:Muramidase / Q000737:chemistry; D019151:Peptide Library; D011208:Powders; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D008024:Ligands; D019151:Peptide Library; D011208:Powders; D011506:Proteins; D009113:Muramidase; D005947:Glucose; D000117:Acetylglucosamine