A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.
Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.
Artero
Jean Baptiste
JB
Institut Laue Langevin, 6 Rue Jules Horowitz, 38042 Grenoble CEDEX 9, France.
Härtlein
Michael
M
McSweeney
Sean
S
Timmins
Peter
P
D000818:Animals; D018360:Crystallography, X-Ray; D003903:Deuterium / Q000737:chemistry*; D017666:Deuterium Oxide; D008958:Models, Molecular; D051381:Rats; D014867:Water; D038222:gamma-Crystallins / Q000737:chemistry*
C107256:crystallin gammaE; D038222:gamma-Crystallins; D014867:Water; D003903:Deuterium; D017666:Deuterium Oxide