Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (d-glycerate dehydrogenase) from Hyphomicrobium methylovorum
| Autor: | Jonathan D. Goldberg, Peter Brick, Masayuki Shimao, Toshio Mitsunaga, Takashi Oshiro, Toyokazu Yoshida, Yoshikazu Izumi |
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| Rok vydání: | 1992 |
| Předmět: |
Crystallography
Bacteria biology Stereochemistry Chemistry Dimer Hydroxypyruvate reductase Dehydrogenase Crystal structure Triclinic crystal system biology.organism_classification law.invention Alcohol Oxidoreductases chemistry.chemical_compound X-Ray Diffraction Structural Biology law Hydroxypyruvate Reductase Methylotroph Glycerate dehydrogenase Crystallization Molecular Biology |
| Zdroj: | Journal of Molecular Biology. 225:909-911 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/0022-2836(92)90410-l |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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