skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Crystallization and preliminary X-ray analysis of Atg10

Abstract

S. cerevisiae Atg10, an E2-like enzyme that mediates the conjugation reaction between Atg12 and Atg5, was crystallized and diffracted to 2.3 Å resolution. 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{sub 1}2{sub 1}2 or P4{sub 3}2{sub 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.

Authors:
; ;  [1];  [2];  [1]
  1. Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812 (Japan)
  2. Division of Molecular Cell Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki 444-8585 (Japan)
Publication Date:
OSTI Identifier:
22363937
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335012; PMID: 17565192; PUBLISHER-ID: pu5182; OAI: oai:pubmedcentral.nih.gov:2335012; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ACETATES; CRYSTALLIZATION; DIFFUSION; INTERFACES; MOLECULES; MONOCRYSTALS; RESOLUTION; SODIUM; SPACE GROUPS

Citation Formats

Yamaguti, Masaya, Suzuki, Nobuo N., Fujioka, Yuko, Ohsumi, Yoshinori, and Inagaki, Fuyuhiko, E-mail: finagaki@pharm.hokudai.ac.jp. Crystallization and preliminary X-ray analysis of Atg10. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107017472.
Yamaguti, Masaya, Suzuki, Nobuo N., Fujioka, Yuko, Ohsumi, Yoshinori, & Inagaki, Fuyuhiko, E-mail: finagaki@pharm.hokudai.ac.jp. Crystallization and preliminary X-ray analysis of Atg10. United Kingdom. doi:10.1107/S1744309107017472.
Yamaguti, Masaya, Suzuki, Nobuo N., Fujioka, Yuko, Ohsumi, Yoshinori, and Inagaki, Fuyuhiko, E-mail: finagaki@pharm.hokudai.ac.jp. Tue . "Crystallization and preliminary X-ray analysis of Atg10". United Kingdom. doi:10.1107/S1744309107017472.
@article{osti_22363937,
title = {Crystallization and preliminary X-ray analysis of Atg10},
author = {Yamaguti, Masaya and Suzuki, Nobuo N. and Fujioka, Yuko and Ohsumi, Yoshinori and Inagaki, Fuyuhiko, E-mail: finagaki@pharm.hokudai.ac.jp},
abstractNote = {S. cerevisiae Atg10, an E2-like enzyme that mediates the conjugation reaction between Atg12 and Atg5, was crystallized and diffracted to 2.3 Å resolution. 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{sub 1}2{sub 1}2 or P4{sub 3}2{sub 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.},
doi = {10.1107/S1744309107017472},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}