Crystallization and preliminary X-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium

Kwang Yeon Hwang, Chun Seok Cho, Sang Suk Kim, Kyuwon Baek, Sung Hou Kim, Yeon Gyu Yu, Yunje Cho

Research output: Contribution to journalArticle

2 Citations (Scopus)

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 languageEnglish
Pages (from-to)927-928
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number4
DOIs
Publication statusPublished - 1999 Apr 1

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium'. Together they form a unique fingerprint.

  • Cite this