Open AccessCloning, purification, crystallization and preliminary X‐ray diffraction crystallographic study of acyl‐protein thioesterase 1 from Saccharomyces cerevisiae
Author(s) -
Yuan Ye,
Wang Xiao,
Li Xu,
Teng Maikun,
Niu Liwen,
Gao Yongxiang
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112019276
Subject(s) - saccharomyces cerevisiae , cloning (programming) , crystallization , recombinant dna , resolution (logic) , diffraction , palmitoylation , crystallography , biology , biochemistry , enzyme , chemistry , gene , physics , organic chemistry , cysteine , artificial intelligence , computer science , optics , programming language
Palmitoylation/depalmitoylation plays an important role in protein modification. yApt1 is the only enzyme in Saccharomyces cerevisiae that catalyses depalmitoylation. In the present study, recombinant full‐length yApt1 was cloned, expressed, purified and crystallized. The crystals diffracted to 2.40 Å resolution and belonged to space group P 4 2 2 1 2, with unit‐cell parameters a = b = 146.43, c = 93.29 Å. A preliminary model of the three‐dimensional structure has been built and further refinement is ongoing.