2a7b
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(New page: 200px<br /><applet load="2a7b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a7b, resolution 1.65Å" /> '''On the Routine Use o...)
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Revision as of 05:50, 21 November 2007
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On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
Overview
Complete and highly redundant data sets were collected at different, wavelengths between 0.80 and 2.65 A for a total of ten different protein, and DNA model systems. The magnitude of the anomalous signal-to-noise, ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be, influenced by the data-collection wavelength and the nature of the, anomalously scattering substructure. By utilizing simple empirical, correlations, for instance between the estimated deltaF/F and the expected, R(anom) or the data-collection wavelength and the expected R(r.i.m.), the, wavelength at which the highest anomalous signal-to-noise ratio can be, expected could be estimated even before the experiment. Almost independent, of the nature of the anomalously scattering substructure and provided that, no elemental X-ray absorption edge is nearby, this optimal wavelength is, 2.1 A.
About this Structure
2A7B is a Single protein structure of sequence from Mus musculus with XE as ligand. Full crystallographic information is available from OCA.
Reference
On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength., Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760
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