Crystallization and preliminary X‐ray diffraction analysis of PAT, an acetyltransferase from Sulfolobus solfataricus

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|64|11|1049-1051

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.64, Iss.11, 2008-11, pp. : 1049-1051

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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 Å resolution on the BL13C1 beamline of NSRRC from a flash‐frozen crystal at 100 K. The crystals belonged to space group P212121, with unit‐cell parameters a = 44.30, b = 46.59, c = 68.39 Å.