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

Content Provider	Europe PMC
Author	Cho, Ching-Chang Luo, Ching-Wei Hsu, Chun-Hua
Copyright Year	2008
Description	PAT, an acetyltransferase from the archaeon S. solfataricus that specifically acetylates the chromatin protein Alba, was expressed, purified and crystallized. 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.
Related Links	https://europepmc.org/backend/ptpmcrender.fcgi?accid=PMC2581692&blobtype=pdf
Volume Number	64
PubMed Central reference number	PMC2581692
Issue Number	Pt 11
Issue Number	pt 11
PubMed reference number	18997339
Journal	Acta Crystallogr Sect F Struct Biol Cryst Commun
e-ISSN	17443091
DOI	10.1107/s1744309108031965
Language	English
Publisher	International Union of Crystallography
Publisher Date	2008-10-31
Access Restriction	Open
Rights License	© International Union of Crystallography 2008
Subject Keyword	hyperthermophilic enzymes acetyltransferases Sulfolobus solfataricus
Content Type	Text
Resource Type	Article
Subject	Biochemistry Condensed Matter Physics Genetics Biophysics Structural Biology