Correlated intramolecular motions and diffuse X-ray scattering in lysozyme.
Correlated motions of protein atoms are of biological significance in processes involving ligand binding, conformational change and information transmission. X-ray scattering patterns from protein crystals contain diffuse scattering that originates from correlated displacements of atoms. Here we present experimental data on diffuse X-ray scattering from lysozyme crystals. We show that the diffuse scattering is similar in form to scattering derived from molecular dynamics simulation and normal mode analysis of the isolated protein, the normal modes giving the closest agreement with experiment.
Faure
P
P
LURE, Laboratoire CNRS-CEA-MEN, Université Paris-Sud, Orsay, France.
Micu
A
A
Pérahia
D
D
Doucet
J
J
Smith
J C
JC
Benoit
J P
JP
D000818:Animals; D002645:Chickens; D018360:Crystallography, X-Ray; D004058:Diffusion; D005260:Female; D015394:Molecular Structure; D009038:Motion; D009113:Muramidase / Q000737:chemistry*; D012542:Scattering, Radiation; D013816:Thermodynamics; D014732:Vibration
D009113:Muramidase