2a7d
From Proteopedia
|
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
2A7D is a Single protein structure of sequence from Gallus gallus with CL, NA and XE as ligands. Active as Lysozyme, with EC number 3.2.1.17 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
Page seeded by OCA on Wed Nov 21 07:57:44 2007
Categories: Gallus gallus | Lysozyme | Single protein | Mueller-Dieckmann, C. | Panjikar, S. | Tucker, P.A. | Weiss, M.S. | CL | NA | XE | Hydrolase
