Crystallization and preliminary X-ray crystallographic studies of glutamate racemase from Lactobacillus fermenti

Ki Seog Lee; Seon Mi Park; Kwang Yeon Hwang; Young Min Chi

doi:10.1107/S1744309104034426

Crystallization and preliminary X-ray crystallographic studies of glutamate racemase from Lactobacillus fermenti

Ki Seog Lee, Seon Mi Park, Kwang Yeon Hwang, Young Min Chi

Department of Biosystems and Biotechnology

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Glutamate racemase catalyzes the conversion of L-glutamic acid to D-glutamic acid and vice versa. Since D-glutamic acid is one of the essential amino acids present in peptidoglycan, glutamate racemase has been considered to be an attractive target for the design of new antibacterial drugs. Glutamate racemase from Lactobacillus fermenti has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant. The crystals belong to the orthorhombic space group C222₁, with unit-cell parameters a = 98.32, b = 184.09, c = 45.99 Å. The asymmetric unit contains one molecule, corresponding to a V_M value of 1.84 Å³ Da^-1. A complete data set has been collected from the native enzyme at 2.28 Å resolution using a synchrotron-radiation source.

Original language	English
Pages (from-to)	199-201
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	61
Issue number	2
DOIs	https://doi.org/10.1107/S1744309104034426
Publication status	Published - 2005

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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Crystallization and preliminary X-ray crystallographic studies of glutamate racemase from Lactobacillus fermenti. / Lee, Ki Seog; Park, Seon Mi; Hwang, Kwang Yeon ; Chi, Young Min.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 2, 2005, p. 199-201.

Research output: Contribution to journal › Article › peer-review

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abstract = "Glutamate racemase catalyzes the conversion of L-glutamic acid to D-glutamic acid and vice versa. Since D-glutamic acid is one of the essential amino acids present in peptidoglycan, glutamate racemase has been considered to be an attractive target for the design of new antibacterial drugs. Glutamate racemase from Lactobacillus fermenti has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant. The crystals belong to the orthorhombic space group C2221, with unit-cell parameters a = 98.32, b = 184.09, c = 45.99 {\AA}. The asymmetric unit contains one molecule, corresponding to a VM value of 1.84 {\AA}3 Da-1. A complete data set has been collected from the native enzyme at 2.28 {\AA} resolution using a synchrotron-radiation source.",

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Crystallization and preliminary X-ray crystallographic studies of glutamate racemase from Lactobacillus fermenti

Abstract

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