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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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 A. The asymmetric unit contains one molecule, corresponding to a Vm value of 2.35 A3 Da-1. Complete data sets from a native and a mercury-derivative crystal have been collected at 2.0 and 2.3 A resolution, respectively, using a synchrotron-radiation source.[1]

References

  1. Crystallization and preliminary x-ray analysis of glutamate racemase from Aquifex pyrophilus, a hyperthermophilic bacterium. Hwang, K.Y., Cho, C.S., Kim, S.S., Baek, K., Kim, S.H., Yu, Y.G., Cho, Y. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
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