Yang, JK Chang, CS Cho, SJ Lee, JY Yu, YG Eom, SH Suh, SW 2024-01-21T09:12:29Z 2024-01-21T09:12:29Z 2021-09-03 2003-03 0907-4449 https://pubs.kist.re.kr/handle/201004/138789 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. English BLACKWELL MUNKSGAARD THERMUS-THERMOPHILUS HB8 CRYSTAL-STRUCTURE SUBSTRATE-SPECIFICITY REFINEMENT PROTEINS COMPLEX FORMS MODE Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii Article 10.1107/S0907444903000076 1 ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, v.59, pp.563 - 565 ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 59 563 565 scie scopus 000181609800032 2-s2.0-0037348392 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article THERMUS-THERMOPHILUS HB8 CRYSTAL-STRUCTURE SUBSTRATE-SPECIFICITY REFINEMENT PROTEINS COMPLEX FORMS MODE crystal aminotransferase methanoccous jannaschii