Open AccessCrystallization and preliminary X‐ray diffraction analysis of PAT, an acetyltransferase from Sulfolobus solfataricus
Author(s) -
Cho ChingChang,
Luo ChingWei,
Hsu ChunHua
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108031965
Subject(s) - sulfolobus solfataricus , crystallization , crystallography , acetyltransferase , beamline , sulfolobus , materials science , chemistry , optics , physics , archaea , biochemistry , acetylation , organic chemistry , gene , beam (structure)
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 Å resolution on the BL13C1 beamline of NSRRC from a flash‐frozen crystal at 100 K. The crystals belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 44.30, b = 46.59, c = 68.39 Å.