Crystallization and preliminary X-ray studies of TON_0559, a putative member of the haloacid dehalogenase (HAD) superfamily from Thermococcus onnurineus NA1.
To elucidate the molecular basis underlying their broad substrate specificity and reaction mechanism of the enzymes belonging to the haloacid dehalogenase (HAD) superfamily, TON_0559, a putative HAD subfamily protein from a hyperthermophilic archaeon Thermococcus onnurineus NA1, was expressed, purified and crystallized. X-ray diffraction data were collected to 2.0 A resolution. The space group is C2, with unit cell parameters a = 121.2 A, b = 62.9 A, c = 37.5 A and beta= 106.5 degrees .
Nguyen
Chi My Thi
CM
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Lee
Hyun Sook
HS
Cho
Yona
Y
Lee
Jung-Hyun
JH
Ha
Sung Chul
SC
Hwang
Hye-Yeon
HY
Kim
Kyeong Kyu
KK
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D019712:Thermococcus / Q000201:enzymology*; D014961:X-Ray Diffraction
D019843:Archaeal Proteins