Crystallization and preliminary X-ray diffraction analysis of PAT, an acetyltransferase from Sulfolobus solfataricus.
PAT is an acetyltransferase from the archaeon Sulfolobus solfataricus that specifically acetylates the chromatin protein Alba. The enzyme was expressed, purified and subsequently crystallized using the sitting-drop vapour-diffusion technique. Native diffraction data were collected to 1.70 A resolution on the BL13C1 beamline of NSRRC from a flash-frozen crystal at 100 K. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.30, b = 46.59, c = 68.39 A.
Cho
Ching Chang
CC
Department and Institute of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan.
Luo
Ching Wei
CW
Hsu
Chun Hua
CH
D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D008969:Molecular Sequence Data; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D000123:Acetyltransferases