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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1049-51. doi: 10.1107/S1744309108031965. Epub 2008 Oct 31.

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

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  • 1Department and Institute of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan.

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.

PMID:
18997339
PMCID:
PMC2581692
DOI:
10.1107/S1744309108031965
[PubMed - indexed for MEDLINE]
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