Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
Crystals of O-acetylserine sulfhydrylase from Aeropyrum pernix K1 were obtained by the hanging-drop vapour-diffusion method at 298 K. An X-ray diffraction data set was collected to 2.25 A resolution at 100 K. The crystal belonged to space group P42(1)2, P4(1)2(1)2, P4(2)2(1)2 or P4(3)2(1)2. The unit-cell parameters were a = b = 74.5, c = 276.0 A. The presence of two subunits of the enzyme per asymmetric unit gives a crystal Volume per protein mass (V(M)) of 2.28 A(3) Da(-1) and a solvent content of 46%(v/v).
Mino
Koshiki
K
Special Division for Human Life Technology, National Institute of Advanced Industrial Science and Technology (AIST, Kansai), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan.
Oda
Yutaka
Y
Ataka
Mitsuo
M
Ishikawa
Kazuhiko
K
D019843:Archaeal Proteins / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D003547:Cysteine Synthase / Q000737:chemistry*; D019620:Desulfurococcaceae / Q000201:enzymology* / Q000235:genetics; D021122:Protein Subunits / Q000737:chemistry; D012997:Solvents / Q000737:chemistry; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D021122:Protein Subunits; D012997:Solvents; D003547:Cysteine Synthase