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Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii

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Abstract
A putative aspartate aminotransferase from the hyperthermophilic archaeon Methanococcus jannaschii encoded by the Mj0684 gene has been overexpressed in Escherichia coli and crystallized at 296 Kusing the sitting-drop vapour-diffusion method. The crystals belong to space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 111.87, c = 60.86 Angstrom. They diffract to 2.2 Angstrom resolution using Cu Kalpha X-rays. The asymmetric unit contains a single subunit of the recombinant Mj0684 gene product, giving a corresponding V-M of 2.25 Angstrom(3) Da(-1) and a solvent content of 45.3% by volume. An X-ray diffraction data set has been collected to 2.2 Angstrom at 295 K.
Author(s)
Yang, JKChang, CSCho, SJLee, JYYu, YGEom, Soo HyunSuh, SW
Issued Date
2003-03
Type
Article
DOI
10.1107/S0907444903000076
URI
https://scholar.gist.ac.kr/handle/local/18379
Publisher
BLACKWELL MUNKSGAARD
Citation
Acta Crystallographica Section D: Biological Crystallography, v.59, no.3, pp.563 - 565
ISSN
0907-4449
Appears in Collections:
Department of Life Sciences > 1. Journal Articles
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