Expression, purification and crystallization of the Atg5-Atg16 complex essential for autophagy.
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 A, beta = 92.1 degrees (form I), a = 79.5, b = 101.4, c = 95.1 A, beta = 98.6 degrees (form II) or a = 56.9, b = 101.2, c = 66.5 A, 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 A. Diffraction data were collected from all crystal forms and high-resolution data to beyond 2.0 A resolution were obtained from a form IV crystal.
Mesh Terms:
Autophagy, Carrier Proteins, Crystallization, Crystallography, X-Ray, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Autophagy, Carrier Proteins, Crystallization, Crystallography, X-Ray, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Date: Oct. 01, 2006
PubMed ID: 17012802
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