Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C.
Selenium-incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit-cell parameters a = 37.58, b = 40.95, c = 48.14 A, alpha = 76.93, beta = 74.04, gamma = 64.05 degrees. Five data sets were collected from a single crystal to 1.6 A using synchrotron radiation for MAD phasing. Self-rotation functions and the Matthews coefficient are consistent with two molecules in the asymmetric unit.
Rehse
Peter H
PH
Highthroughput Factory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
Nodake
Yuichi
Y
Kuroishi
Chizu
C
Tahirov
Tahir H
TH
D003461:Crystallography; D018360:Crystallography, X-Ray; D019992:Databases as Topic; D004926:Escherichia coli / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011486:Protein C / Q000378:metabolism*; D012643:Selenium / Q000737:chemistry; D017356:Synchrotrons; D013696:Temperature; D016963:Thermus thermophilus / Q000378:metabolism*
D011486:Protein C; D012643:Selenium