title: Crystallization and preliminary X-ray diffraction analysis of PAT, an acetyltransferase from Sulfolobus solfataricus.
abstract: 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.
authors.affiliation: Department and Institute of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan.
authors.forename: Ching Chang
authors.initials: CC
authors.lastname: Cho
authors.forename: Ching Wei
authors.initials: CW
authors.lastname: Luo
authors.forename: Chun Hua
authors.initials: CH
authors.lastname: Hsu
mesh_terms: 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
chemical_list: D019843:Archaeal Proteins; D000123:Acetyltransferases