The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Crystallization of Mouse Lung Carbonyl Reductase Complexed with NADPH and Analysis of Symmetry of Its Tetrameric Molecule
Nobutada TanakaTakamasa NonakaMasayuki NakanishiYoshihiro DeyashikiAkira HaraYukio Mitsui
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1995 年 118 巻 5 号 p. 871-873

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抄録
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 a=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.
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© The Japanese Biochemical Society
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