Literature DB >> 1602490

Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (D-glycerate dehydrogenase) from Hyphomicrobium methylovorum.

J D Goldberg1, P Brick, T Yoshida, T Mitsunaga, T Oshiro, M Shimao, Y Izumi.   

Abstract

Two crystal forms of hydroxypyruvate reductase (D-glycerate dehydrogenase) from the methylotrophic bacterium Hyphomicrobium methylovorum have been grown from ammonium sulphate solutions. One crystal form is triclinic, with unit cell parameters a = 60.4 A, b = 60.5 A, c = 66.3 A, alpha = 102.3 degrees, beta = 113.7 degrees and gamma = 102.7 degrees, suggesting that a dimer (monomer M(r) 38,000) occupies the unit cell. This crystal form diffracts to beyond 2.4 A resolution and is suitable for crystallographic structure analysis.

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Year:  1992        PMID: 1602490     DOI: 10.1016/0022-2836(92)90410-l

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  1 in total

Review 1.  L-serine production by a methylotroph and its related enzymes.

Authors:  Y Izumi; T Yoshida; S S Miyazaki; T Mitsunaga; T Ohshiro; M Shimao; A Miyata; T Tanabe
Journal:  Appl Microbiol Biotechnol       Date:  1993-07       Impact factor: 4.813

  1 in total

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