A comparison of refined X-ray structures of hydrogenated and perdeuterated rat γE-crystallin in H2O and D2O

✍ Scribed by Artero, Jean-Baptiste ;Härtlein, Michael ;McSweeney, Sean ;Timmins, Peter

• Book ID: 104478154
• Publisher: International Union of Crystallography
• Year: 2005
• Tongue: English
• Weight: 866 KB
• Volume: 61
• Category: Article
• ISSN: 0907-4449
• DOI: 10.1107/s0907444905028532

✦ Synopsis

Rat E-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 -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.