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

Authors
Yang, JKChang, CSCho, SJLee, JYYu, YGEom, SHSuh, SW
Issue Date
2003-03
Publisher
BLACKWELL MUNKSGAARD
Citation
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.59, pp.563 - 565
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.
Keywords
THERMUS-THERMOPHILUS HB8; CRYSTAL-STRUCTURE; SUBSTRATE-SPECIFICITY; REFINEMENT; PROTEINS; COMPLEX; FORMS; MODE; THERMUS-THERMOPHILUS HB8; CRYSTAL-STRUCTURE; SUBSTRATE-SPECIFICITY; REFINEMENT; PROTEINS; COMPLEX; FORMS; MODE; crystal; aminotransferase; methanoccous jannaschii
ISSN
0907-4449
URI
https://pubs.kist.re.kr/handle/201004/138789
DOI
10.1107/S0907444903000076
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KIST Article > 2003
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