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Title: Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase

Abstract

Human Rad has been crystallized. A diffraction data set was collected to a resolution of 1.8 Å. Human Rad is a new member of the Ras GTPase superfamily and is overexpressed in human skeletal muscle of individuals with type II diabetes. The GTPase core domain was overexpressed in Escherichia coli and purified for crystallization. Crystals were obtained at 293 K by vapour diffusion using a crystallization robot. The crystals were found to belong to space group P2{sub 1}, with unit-cell parameters a = 52.2, b = 58.6, c = 53.4 Å, β = 97.9°, and contained two Rad molecules in the crystallographic asymmetric unit. A diffraction data set was collected to a resolution of 1.8 Å using synchrotron radiation at SPring-8.

Authors:
; ;  [1];  [1];  [2]
  1. Structural Biology Laboratory, Nara Institute of Science and Technology (Japan)
  2. (Japan)
Publication Date:
OSTI Identifier:
22356173
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 61; Journal Issue: Pt 11; Other Information: PMCID: PMC1978125; PMID: 16511212; PUBLISHER-ID: fw5048; OAI: oai:pubmedcentral.nih.gov:1978125; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; ESCHERICHIA COLI; MOLECULES; RESOLUTION; SPACE GROUPS; SYNCHROTRON RADIATION

Citation Formats

Yanuar, Arry, Sakurai, Shigeru, Kitano, Ken, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309105031982.
Yanuar, Arry, Sakurai, Shigeru, Kitano, Ken, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, & CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase. United Kingdom. doi:10.1107/S1744309105031982.
Yanuar, Arry, Sakurai, Shigeru, Kitano, Ken, Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp, and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192. Tue . "Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase". United Kingdom. doi:10.1107/S1744309105031982.
@article{osti_22356173,
title = {Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase},
author = {Yanuar, Arry and Sakurai, Shigeru and Kitano, Ken and Hakoshima, Toshio, E-mail: hakosima@bs.naist.jp and CREST, Japan Science and Technology Agency, Keihanna Science City, Nara 630-0192},
abstractNote = {Human Rad has been crystallized. A diffraction data set was collected to a resolution of 1.8 Å. Human Rad is a new member of the Ras GTPase superfamily and is overexpressed in human skeletal muscle of individuals with type II diabetes. The GTPase core domain was overexpressed in Escherichia coli and purified for crystallization. Crystals were obtained at 293 K by vapour diffusion using a crystallization robot. The crystals were found to belong to space group P2{sub 1}, with unit-cell parameters a = 52.2, b = 58.6, c = 53.4 Å, β = 97.9°, and contained two Rad molecules in the crystallographic asymmetric unit. A diffraction data set was collected to a resolution of 1.8 Å using synchrotron radiation at SPring-8.},
doi = {10.1107/S1744309105031982},
journal = {Acta Crystallographica. Section F},
number = Pt 11,
volume = 61,
place = {United Kingdom},
year = {Tue Nov 01 00:00:00 EST 2005},
month = {Tue Nov 01 00:00:00 EST 2005}
}
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