2a7d: Difference between revisions
No edit summary |
No edit summary |
||
Line 2: | Line 2: | ||
<StructureSection load='2a7d' size='340' side='right' caption='[[2a7d]], [[Resolution|resolution]] 1.66Å' scene=''> | <StructureSection load='2a7d' size='340' side='right' caption='[[2a7d]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2a7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A7D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a7d RCSB], [http://www.ebi.ac.uk/pdbsum/2a7d PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7d OCA], [http://pdbe.org/2a7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a7d RCSB], [http://www.ebi.ac.uk/pdbsum/2a7d PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Line 27: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2a7d" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Line 34: | Line 35: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Chick]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Mueller-Dieckmann, C]] | [[Category: Mueller-Dieckmann, C]] |
Revision as of 07:13, 11 September 2015
On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection WavelengthOn the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
Structural highlights
Function[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedComplete 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|