Crystallization and preliminary X-ray crystallographic studies of phosphoglycerate kinase from Thermus caldophilus.
We report the purification and crystallization of phosphoglycerate kinase from Thermus caldophilus (Tca). The enzyme crystallizes in the P2(1)2(1)2(1) space group (cell dimensions a = 65.1, b = 71.3, c = 80.2 A), with one molecule in the asymmetric unit. A complete set of diffraction data was collected from an orthorhombic crystal up to 1.8 A resolution.
Lee
Jun Hyuck
JH
Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.
Im
Young Jun
YJ
Rho
Seong-Hwan
SH
Park
Seong Ho
SH
Kang
Gil Bu
GB
Cho
Su Jin
SJ
Kim
Tae-Yeon
TY
Shin
Hyun-Jae
HJ
Lee
Dae-Sil
DS
Eom
Soo Hyun
SH
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000302:isolation & purification; D013824:Thermus / Q000201:enzymology*
D010735:Phosphoglycerate Kinase