期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 70, 期 -, 页码 611-615出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14006815
关键词
-
资金
- 973 Program [2014CB910201]
- National Natural Science Foundation of China [31270815, 31100527]
The protein 26S proteasome regulatory subunit p27 is one of the four chaperones that help in the assembly of the 19S regulatory particle (RP) of the 26S proteasome. In the present work, the N-terminus of p27 (residues 1-128) from Mus musculus was cloned, expressed, purified and crystallized alone and in complex with the C-terminal ATPase domain of Rpt5 (residues 173-442). The crystals of p27 (1-128) diffracted to 1.7 angstrom resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 26.79, b = 30.39, c = 145.06 A. Resolution-dependent Matthews coefficient probability analysis suggested the presence of only one molecule per asymmetric unit, with 40.5% solvent content and a V-M value of 2.02 angstrom(3) Da(-1). The crystal of the p27((1-128))-Rpt5((173-442)) complex diffracted to 4 angstrom resolution and belonged to space group P222, with unit-cell parameters a = 75.93, b = 76.08, c = 336.85 angstrom. The presence of four heterodimers in the asymmetric unit with 53.2% solvent content and a V-M value of 2.63 angstrom(3) Da(-1) or five heterodimers in the asymmetric unit with 41.5% solvent content and a V-M value of 2.10 angstrom(3) Da(-1) is assumed.
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