Open AccessCrystallization and preliminary X‐ray analysis of Atg10
Author(s) -
Yamaguti Masaya,
Suzuki Nobuo N.,
Fujioka Yuko,
Ohsumi Yoshinori,
Inagaki Fuyuhiko
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107017472
Subject(s) - atg5 , crystallization , atg12 , saccharomyces cerevisiae , crystallography , polyethylene glycol , materials science , autophagy , biology , biochemistry , yeast , chemistry , organic chemistry , apoptosis
Atg10 is an E2‐like enzyme that catalyzes the conjugation reaction between Atg12 and Atg5. The Atg12–Atg5 conjugate is essential for autophagy, the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. Microcrystals of Saccharomyces cerevisiae Atg10 were obtained by the free‐interface diffusion method using polyethylene glycol and sodium acetate as precipitants. Using these precipitants, large crystals suitable for data collection were obtained using the sitting‐drop vapour‐diffusion method. The crystals belong to space group P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 51.61, c = 256.16 Å, and are estimated to contain two protein molecules per asymmetric unit. A native data set was collected to 2.3 Å resolution from a single crystal.