Published December 20, 2007 | Version v1
Journal article

Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans

  • 1. National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871 (China)
  • 2. Rigaku/MSC Inc., 9009 New Trails Drive, The Woodlands, TX 77381 (United States)
  • 3. Shenzhen Graduate School of Peking University, Shenzhen 518055 (China)

Description

SMU.573 from S. mutans was expressed in E. coli and crystallized. The crystals belong to space group I4 and 2.5 Å resolution diffraction data were collected at an in-house chromium radiation source. SMU.573 from Streptococcus mutans is a structurally and functionally uncharacterized protein that was selected for structural biology studies. Native and SeMet-labelled proteins were expressed with an N-His tag in Escherichia coli BL21 (DE3) and purified by Ni2+-chelating and size-exclusion chromatography. Crystals of the SeMet-labelled protein were obtained by the hanging-drop vapour-diffusion method and a 2.5 Å resolution diffraction data set was collected using an in-house chromium radiation source. The crystals belong to space group I4, with unit-cell parameters a = b = 96.53, c = 56.26 Å, α = β = γ = 90°

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309107065645; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373987

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
64
Journal Issue
Pt 1
Journal Page Range
p. 47-49
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2008
Notes
PMCID: PMC2373987; PMID: 18097102; PUBLISHER-ID: bo5032; OAI: oai:pubmedcentral.nih.gov:2373987