title: Crystallization and preliminary analysis of telokin, the C-terminal domain of myosin light chain kinase.
abstract: Telokin, an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase from turkey gizzard has been crystallized in a form suitable for a high-resolution diffraction analysis. The crystals were grown from solutions of polyethylene glycol 8000 using the hanging-drop vapor diffusion method. They belong to the trigonal space group P3(1)21 or P3(2)21 with cell parameters a = 64.0 A, c = 59.4 A and diffract to at least 2.7 A resolution.
authors.affiliation: Institute for Enzyme Research, Graduate School, University of Wisconsin, Madison 53705.
authors.forename: T A
authors.initials: TA
authors.lastname: Anderson
authors.forename: M
authors.initials: M
authors.lastname: Ito
authors.forename: D J
authors.initials: DJ
authors.lastname: Hartshorne
authors.forename: I
authors.initials: I
authors.lastname: Rayment
mesh_terms: D000818:Animals; D003460:Crystallization; D009124:Muscle Proteins / Q000737:chemistry*; D009219:Myosin-Light-Chain Kinase / Q000737:chemistry* / Q000378:metabolism; D010446:Peptide Fragments; D010455:Peptides; D014422:Turkeys; D014961:X-Ray Diffraction
chemical_list: D009124:Muscle Proteins; D010446:Peptide Fragments; D010455:Peptides; C060640:telokin; D009219:Myosin-Light-Chain Kinase