Cho Ching Chang, Luo Ching Wei, Hsu Chun Hua
Department and Institute of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1049-51. doi: 10.1107/S1744309108031965. Epub 2008 Oct 31.
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.
PAT是一种来自嗜热栖热菌的乙酰转移酶，它能特异性地使染色质蛋白Alba发生乙酰化。该酶经过表达、纯化，随后采用坐滴气相扩散技术进行结晶。在NSRRC的BL13C1光束线上，从100 K下快速冷冻的晶体收集到了分辨率为1.70 Å的原生衍射数据。晶体属于空间群P2(1)2(1)2(1)，晶胞参数为a = 44.30、b = 46.59、c = 68.39 Å。
