Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii
- Authors
- Yang, JK; Chang, CS; Cho, SJ; Lee, JY; Yu, YG; Eom, SH; Suh, 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
- Appears in Collections:
- KIST Article > 2003
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