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Nobutada Tanaka, Takamasa Nonaka, Masayuki Nakanishi, Yoshihiro Deyashiki, Akira Hara, Yukio Mitsui, Crystallization of Mouse Lung Carbonyl Reductase Complexed with NADPH and Analysis of Symmetry of Its Tetrameric Molecule, The Journal of Biochemistry, Volume 118, Issue 5, October 1995, Pages 871–873, https://doi.org/10.1093/jb/118.5.871
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Abstract
Mouse lung carbonyl reductase (MLCR), which belongs to the short-chain dehydrogenase/reductase family, is an oxidoreductase involved in the metabolism of biogenic and xenobiotic carbonyl compounds. The crystals of MLCR complexed with its cofactor NADPH belong to a monoclinic space group P21 with dimensions α=79.73 Å, b=105.5 Å, c=60.87 Å, and β=91.43°. X-ray diffraction data were collected up to 1.8 Å resolution using a macromolecule-oriented Weissenberg camera at the Photon Factory synchrotron radiation source. Studies using a self-rotation function revealed the presence of a twofold rotational symmetry relating the subunits. This suggests that the tetrameric MLCR molecule has the 222 point group symmetry.