2a7b
From Proteopedia
(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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| - | [[Image:2a7b.gif|left|200px]]<br /><applet load="2a7b" size=" | + | [[Image:2a7b.gif|left|200px]]<br /><applet load="2a7b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a7b, resolution 1.65Å" /> | caption="2a7b, resolution 1.65Å" /> | ||
'''On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength'''<br /> | '''On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Complete and highly redundant data sets were collected at different | + | 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== | ==About this Structure== | ||
| - | 2A7B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with XE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2A7B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=XE:'>XE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mueller-Dieckmann, C.]] | [[Category: Mueller-Dieckmann, C.]] | ||
[[Category: Panjikar, S.]] | [[Category: Panjikar, S.]] | ||
| - | [[Category: Tucker, P | + | [[Category: Tucker, P A.]] |
| - | [[Category: Weiss, M | + | [[Category: Weiss, M S.]] |
[[Category: XE]] | [[Category: XE]] | ||
[[Category: protein transport]] | [[Category: protein transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:18 2008'' |
Revision as of 14:24, 21 February 2008
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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 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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