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

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 P6(1)22 or P6(5)22 with unit-cell parameters a = b = 72.1, c = 185.02 Angstrom. The asymmetric unit contains one molecule, corresponding to a V-m value of 2.35 Angstrom(3) Da(-1). Complete data sets from a native and a mercury-derivative crystal have been collected at 2.0 and 2.3 Angstrom resolution, respectively, using a synchrotron-radiation source.