Open AccessCrystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor
Author(s) -
Koháryová Michaela,
Brynda Jiří,
Řezáčová Pavlína,
Kollárová Marta
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111021385
Subject(s) - streptomyces coelicolor , thioredoxin , thioredoxin reductase , monoclinic crystal system , ferredoxin thioredoxin reductase , chemistry , crystallography , biochemistry , enzyme , crystal structure , gene , mutant
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 P 2 1 , with unit‐cell parameters a = 82.9, b = 60.6, c = 135.4 Å, α = γ = 90.0, β = 96.5°.