title: Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor.
abstract: Thioredoxin reductases are homodimeric flavoenzymes that catalyze the transfer of electrons from NADPH to oxidized thioredoxin substrate. Bacterial thioredoxin reductases represent a promising target for the development of new antibiotics. Recombinant thioredoxin reductase TrxB from Streptomyces coelicolor was crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from cryocooled crystals to 2.4 Å resolution using a synchrotron-radiation source. The crystals belonged to the primitive monoclinic space group P2(1), with unit-cell parameters a = 82.9, b = 60.6, c = 135.4 Å, α = γ = 90.0, β = 96.5°.
authors.affiliation: Faculty of Natural Sciences, Department of Biochemistry, Commenius University, Bratislava, Slovakia.
authors.forename: Michaela
authors.initials: M
authors.lastname: Koháryová
authors.forename: Jiří
authors.initials: J
authors.lastname: Brynda
authors.forename: Pavlína
authors.initials: P
authors.lastname: Rezáčová
authors.forename: Marta
authors.initials: M
authors.lastname: Kollárová
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D048372:Streptomyces coelicolor / Q000201:enzymology*; D013880:Thioredoxin-Disulfide Reductase / Q000737:chemistry*
chemical_list: D013880:Thioredoxin-Disulfide Reductase