title: Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K.
abstract: Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P2(1), with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K.
authors.affiliation: RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
authors.forename: Takayuki
authors.initials: T
authors.lastname: Motoyama
authors.forename: Masayoshi
authors.initials: M
authors.lastname: Nakasako
authors.forename: Isamu
authors.initials: I
authors.lastname: Yamaguchi
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry* / Q000235:genetics; D009154:Mutation; D011487:Protein Conformation
chemical_list: D006836:Hydro-Lyases; C082741:scytalone dehydratase