Published March 24, 2005 | Version v1
Journal article

Expression, purification and crystallization of a human protein SH3BGRL at atomic resolution

  • 1. Graduate School of the Chinese Academy of Sciences, Beijing 100039 (China)
  • 2. Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Science, Beijing 100101 (China)
  • 3. Shanghai Institute of Hematology, Rui Jin Hospital, Shanghai Second Medical University, Shanghai 200025 (China)

Description

The protein SH3BGRL, containing both SH3-binding and Homer EVH1-binding motifs, has been crystallized using the hanging-drop vapour-diffusion method. The protein SH3BGRL, containing both SH3-binding and Homer EVH1-binding motifs, has been crystallized using the hanging-drop vapour-diffusion method. The crystals diffract to 0.88 Å resolution and belong to space group P212121, with unit-cell parameters a = 28.8886, b = 34.9676, c = 98.0016 Å. Preliminary analysis indicates that the asymmetric unit contains one molecule and has a solvent content of about 34%

Availability note (English)

Available from http://dx.doi.org/10.1107/S174430910500730X; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952435

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
61
Journal Issue
Pt 4
Journal Page Range
p. 384-386
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46069246
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTALLIZATION; CRYSTALS; DIFFUSION; MOLECULES; PROTEINS; RESOLUTION; SOLVENTS; SPACE GROUPS
Descriptors DEC
ORGANIC COMPOUNDS; PHASE TRANSFORMATIONS; SYMMETRY GROUPS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2005
Notes
PMCID: PMC1952435; PMID: 16511048; PUBLISHER-ID: pu5067; OAI: oai:pubmedcentral.nih.gov:1952435