Published December 21, 2010 | Version v1
Journal article

Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain

  • 1. Biostructural Research, Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen (Denmark)

Description

The human G3BP1 NTF2-like domain was crystallized. Diffraction data were collected to 3.6 Å resolution. The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6322, with unit-cell parameters a = b = 89.84, c = 70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309110042156; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3079970

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
67
Journal Issue
Pt 1
Journal Page Range
p. 48-50
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2011
Notes
PMCID: PMC3079970; PMID: 21206022; PUBLISHER-ID: hc5113; OAI: oai:pubmedcentral.nih.gov:3079970