Related Experiment Video
Updated: Jun 15, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Crystallization and preliminary X-ray studies of ferredoxin-NADP+ oxidoreductase encoded by Bacillus subtilis yumC
Hirofumi Komori1, Daisuke Seo, Takeshi Sakurai
1Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
Abstract:
Ferredoxin-NADP(+) oxidoreductase encoded by Bacillus subtilis yumC has been purified and successfully crystallized in complex with NADP(+) in two forms. Diffraction data from crystals of these two forms were collected at resolutions of 1.8 and 1.9 A. The former belonged to space group P2(1)2(1)2, with unit-cell parameters a = 63.90, b = 135.72, c = 39.19 A, and the latter to space group C2, with unit-cell parameters a = 207.47, b = 64.85, c = 61.12 A, beta = 105.82 degrees. The initial structure was determined by the molecular-replacement method using a thioredoxin reductase-like protein as a search model.

