Crystallization and preliminary X-ray analysis of the Mj0684 gene product, a putative aspartate aminotransferase, from Methanococcus jannaschii.
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 K using 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 A. They diffract to 2.2 A 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 A(3) Da(-1) and a solvent content of 45.3% by Volume. An X-ray diffraction data set has been collected to 2.2 A at 295 K.
Yang
Jin Kuk
JK
Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea.
Chang
Changsoo
C
Cho
Seung-Je
SJ
Lee
Jae Young
JY
Yu
Yeon Gyu
YG
Eom
Soo Hyun
SH
Suh
Se Won
SW
D001219:Aspartate Aminotransferases / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D008027:Light; D017017:Methanococcus / Q000201:enzymology* / Q000235:genetics*; D012542:Scattering, Radiation
D001219:Aspartate Aminotransferases