title: Purification, crystallization and preliminary X-ray analysis of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8.
abstract: Fumarylacetoacetase catalyzes the final step of tyrosine and phenylalanine catabolism. A recombinant form of the fumarylacetoacetase family member TTHA0809 from Thermus thermophilus HB8 has been crystallized by the oil-microbatch method using sodium chloride as a precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 93.3, b = 73.4, c = 122.6 A, beta = 111.8 degrees. The crystals are most likely to contain two dimers in the asymmetric unit, with a V(M) value of 3.32 A3 Da(-1). Diffraction data were collected at 2.2 A resolution using synchrotron radiation at beamline BL26B1 of SPring-8, Japan.
authors.affiliation: Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cyo, Sayo-gun, Hyogo 679-5148, Japan.
authors.forename: Hisashi
authors.initials: H
authors.lastname: Mizutani
authors.forename: Naoki
authors.initials: N
authors.lastname: Kunishima
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D006867:Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D008027:Light; D012542:Scattering, Radiation; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D006867:Hydrolases; C020156:fumarylacetoacetase