TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of the Rho-binding domain of bovine Rho-kinase
AU - Ihara, Kentaro
AU - Shimizu, Toshiyuki
AU - Maesaki, Ryoko
AU - Okada, Kengo
AU - Amano, Mutsuki
AU - Kaibuchi, Kozo
AU - Hakoshima, Toshio
PY - 2000
Y1 - 2000
N2 - Rho-kinase binds to a small GTPase Rho in a GTP-dependent manner and regulates many cytoskeletal events in the cell. The minimum region of bovine Rho-kinase sufficient for Rho-binding was expressed as a fusion protein with glutathione S-transferase. After removal of the glutathione S-transferase, thin plate crystals were obtained. The selenomethionine-substituted protein was 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 unit-cell parameters a = 148.0 (2), b = 26.1 (1), c = 39.6 (1) Å, β = 90.3 (1)°. The crystals diffract to a resolution beyond 1.5 Å.
AB - Rho-kinase binds to a small GTPase Rho in a GTP-dependent manner and regulates many cytoskeletal events in the cell. The minimum region of bovine Rho-kinase sufficient for Rho-binding was expressed as a fusion protein with glutathione S-transferase. After removal of the glutathione S-transferase, thin plate crystals were obtained. The selenomethionine-substituted protein was 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 unit-cell parameters a = 148.0 (2), b = 26.1 (1), c = 39.6 (1) Å, β = 90.3 (1)°. The crystals diffract to a resolution beyond 1.5 Å.
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U2 - 10.1107/S0907444900007174
DO - 10.1107/S0907444900007174
M3 - Article
C2 - 10944348
AN - SCOPUS:0033875808
SN - 0907-4449
VL - 56
SP - 1042
EP - 1044
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 8
ER -