Crystallization and preliminary X-ray analysis of Atg3.

Yuya Yamada, Nobuo N Suzuki, Yuko Fujioka, Yoshinobu Ichimura, Yoshinori Ohsumi, Fuyuhiko Inagaki

Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62(Pt 10) , 1016-7, (2006)

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Abstract

Atg3 is an E2-like enzyme that catalyzes the conjugation reaction between Atg8 and phosphatidylethanolamine (PE). The Atg8-PE conjugate is essential for autophagy, the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. Crystals of Saccharomyces cerevisiae Atg3 have been obtained by the sitting-drop vapour-diffusion method using ammonium sulfate and lithium sulfate as precipitants. A native data set was collected from a single crystal to 2.5 A resolution. The crystals belong to space group P4(1) or P4(3), with unit-cell parameters a = 59.33, c = 115.22 A, and are expected to contain one protein molecule per asymmetric unit.