title: Crystallization and preliminary X-ray analysis of Atg10.
abstract: 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 P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 51.61, c = 256.16 A, and are estimated to contain two protein molecules per asymmetric unit. A native data set was collected to 2.3 A resolution from a single crystal.
authors.affiliation: Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812, Japan.
authors.forename: Masaya
authors.initials: M
authors.lastname: Yamaguti
authors.forename: Nobuo N
authors.initials: NN
authors.lastname: Suzuki
authors.forename: Yuko
authors.initials: Y
authors.lastname: Fujioka
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Ohsumi
authors.forename: Fuyuhiko
authors.initials: F
authors.lastname: Inagaki
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D029701:Saccharomyces cerevisiae Proteins