Open AccessCrystallization and preliminary X‐ray analysis of Atg3
Author(s) -
Yamada Yuya,
Suzuki Nobuo N.,
Fujioka Yuko,
Ohsumi Yoshinori,
Ichimura Yoshinobu,
Inagaki Fuyuhiko
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106036098
Subject(s) - crystallization , materials science , x ray , crystallography , chemistry , physics , optics , thermodynamics
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 Å resolution. The crystals belong to space group P 4 1 or P 4 3 , with unit‐cell parameters a = 59.33, c = 115.22 Å, and are expected to contain one protein molecule per asymmetric unit.