Open AccessCrystallization of the coiled‐coil domain of Atg16 essential for autophagy
Author(s) -
Fujioka Yuko,
Noda Nobuo N.,
Matsushita Minako,
Ohsumi Yoshinori,
Inagaki Fuyuhiko
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108031898
Subject(s) - crystallization , coiled coil , domain (mathematical analysis) , autophagy , crystallography , materials science , biophysics , chemistry , biology , biochemistry , mathematics , mathematical analysis , apoptosis , organic chemistry
Atg16 is a scaffold protein that interacts with Atg12–Atg5 protein conjugates via its N‐terminal domain and self‐assembles via its coiled‐coil domain, thus forming a multimeric Atg12–Atg5–Atg16 complex that is essential for autophagy. The coiled‐coil domain of Atg16 was expressed, purified and crystallized. The crystal belonged to space group P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = 127.7, c = 77.8 Å. Self‐rotation functions and volume‐to‐weight ratio values suggested that the crystal may contain six molecules per asymmetric unit. Since the domain does not contain a methionine residue, selenomethionine‐labelled crystals were prepared with a leucine‐to‐methionine substitution in the coiled‐coil domain and these crystals were used for the collection of single‐wavelength anomalous dispersion data to 2.5 Å resolution.