Crystallization and preliminary crystallographic analysis of the Rho-binding domain of bovine Rho-kinase

Citation
K. Ihara et al., Crystallization and preliminary crystallographic analysis of the Rho-binding domain of bovine Rho-kinase, ACT CRYST D, 56, 2000, pp. 1042-1044
Citations number
18
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
8
Pages
1042 - 1044
Database
ISI
SICI code
0907-4449(200008)56:<1042:CAPCAO>2.0.ZU;2-P
Abstract
Rho-kinase binds to a small GTPase Rho in a GTP-dependent manner and regula tes many cytoskeletal events in the cell. The minimum region of bovine Rho- kinase sufficient for Rho-binding was expressed as a fusion protein with gl utathione S-transferase. After removal of the glutathione S-transferase, th in plate crystals were obtained. The selenomethionine-substituted protein w as introduced and crystallized, as was the native protein. The crystals of the Rho-binding domain of Rho-kinase belong to the space group C2, with uni t-cell parameters a = 148.0 (2), b = 26.1 (1), c = 39.6 (1) Angstrom, beta = 90.3 (1)degrees. The crystals diffract to a resolution beyond 1.5 Angstro m.