Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/67796
標題: Crystallization and preliminary X-ray diffraction analysis of PAT, an acetyltransferase from Sulfolobus solfataricus
作者: Cho, C.C.
Luo, C.W.
Hsu, C.H.
關鍵字: chromatin protein;archaeal;sir2;alba
Project: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
期刊/報告no:: Acta Crystallographica Section F-Structural Biology and Crystallization Communications, Volume 64, Page(s) 1049-1051.
摘要: 
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 angstrom 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 angstrom.
URI: http://hdl.handle.net/11455/67796
ISSN: 1744-3091
DOI: 10.1107/s1744309108031965
Appears in Collections:期刊論文

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