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

Authors :
Jonathan D. Goldberg
Peter Brick
Masayuki Shimao
Toshio Mitsunaga
Takashi Oshiro
Toyokazu Yoshida
Yoshikazu Izumi
Source :
Journal of Molecular Biology. 225:909-911
Publication Year :
1992
Publisher :
Elsevier BV, 1992.

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.

Details

ISSN :
00222836
Volume :
225
Database :
OpenAIRE
Journal :
Journal of Molecular Biology
Accession number :
edsair.doi.dedup.....5f04a011e48a78dfa7d15e7e453dbb89
Full Text :
https://doi.org/10.1016/0022-2836(92)90410-l