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Structure determination of VEGF-E by sulfur SAD.

  • 2006-10-24
Published in:
  • Acta crystallographica. Section D, Biological crystallography. - 2006
Crystallography, X-Ray
Disulfides
Humans
Models, Molecular
Protein Structure, Tertiary
Sulfur
Vascular Endothelial Growth Factor A
English The crystal structure of VEGF-E was solved by the sulfur single-wavelength anomalous dispersion method (S-SAD) using highly redundant low-resolution data collected at a wavelength of lambda approximately 1.7 A with an estimated anomalous signal of 1.5%. 11 sulfur sites, nine out of 16 disulfide bonds and two out of 12 methionines could be located in the asymmetric unit using data truncated at a resolution of 4.1 A; however, none of the common diffraction data-quality indicators for SAD allowed clear discrimination between successful and unsuccessful resolution cutoffs. The high solvent content of 75% allowed efficient density modification to be performed and an unbiased electron-density map of good quality to be generated. This study demonstrates the strength of S-SAD for phasing using accurate highly redundant data at low resolution.
Language
  • English
Open access status
green
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Persistent URL
https://sonar.ch/global/documents/278403
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