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

Kentaro Ihara, Toshiyuki Shimizu, Ryoko Maesaki, Kengo Okada, Mutsuki Amano, Kozo Kaibuchi, Toshio Hakoshima

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1042-1044
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number8
DOIs
Publication statusPublished - 29-08-2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology

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