title: Cloning, purification, crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae.
abstract: 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 P4(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.
authors: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors: Ye
authors: Y
authors: Yuan
authors: Xiao
authors: X
authors: Wang
authors: Xu
authors: X
authors: Li
authors: Maikun
authors: M
authors: Teng
authors: Liwen
authors: L
authors: Niu
authors: Yongxiang
authors: Y
authors: Gao
mesh_terms: D002850:Chromatography, Gel; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D013869:Thiolester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D013869:Thiolester Hydrolases; C485726:YLR118C protein, S cerevisiae