Abstract
Glutamate racemase catalyzes the reversible reaction of L.-glutamate to D-glutamate, an essential component of the bacterial cell wall. Glutamate racemase from Aquifex pyrophilus has been crystallized by the hanging-drop vapor-diffusion method using polyethylene glycol 6000 as a precipitant. The crystals belong to space group P6122 or P6522 with unit-cell parameters a = b = 72.1, c = 185.02 Å. The asymmetric unit contains one molecule, corresponding to a V(m) value of 2.35 Å3 Da-1. Complete data sets from a native and a mercury-derivative crystal have been collected at 2.0 and 2.3 Å resolution, respectively, using a synchrotron-radiation source.
| Original language | English |
|---|---|
| Pages (from-to) | 927-928 |
| Number of pages | 2 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 55 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1999 Apr 1 |
ASJC Scopus subject areas
- Structural Biology
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Hwang, K. Y., Cho, C. S., Kim, S. S., Baek, K., Kim, S. H., Yu, Y. G., & Cho, Y. (1999). Crystallization and preliminary X-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium. Acta Crystallographica Section D: Biological Crystallography, 55(4), 927-928. https://doi.org/10.1107/S0907444999000608