Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 62, Issue -, Pages 1021-1023Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309106036232
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Atg5 is a novel 34 kDa protein that is covalently modified by Atg12, a ubiquitin-like modifier, and forms a complex with Atg16. The Atg12-Atg5-Atg16 complex localizes to autophagosome precursors and plays an essential role in autophagosome formation. Saccharomyces cerevisiae Atg5 in complex with the N-terminal regions of Atg16 was expressed, purified and crystallized in four crystal forms. Forms I, II and III belong to space group P2(1), with unit-cell parameters a = 66.3, b = 104.4, c = 112.1 angstrom, beta = 92.1 degrees (form I), a= 79.5, b = 101.4, c = 95.1 angstrom, beta = 98.6 degrees (form II) or a = 56.9, b = 101.2, c = 66.5 angstrom, beta = 100.6 degrees (form III). Form IV belongs to space group P4(2)2(1)2, with unit-cell parameters a = 73.3, c = 148.1 angstrom. Diffraction data were collected from all crystal forms and high-resolution data to beyond 2.0 angstrom resolution were obtained from a form IV crystal.
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