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Updated: May 30, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
Published on: March 11, 2022
Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor
Michaela Koháryová1, Jiří Brynda, Pavlína Rezáčová
1Faculty of Natural Sciences, Department of Biochemistry, Commenius University, Bratislava, Slovakia.
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°.
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