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New page: left|200px<br /><applet load="2a7a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a7a, resolution 1.75Å" /> '''On the Routine Use o...
 
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[[Image:2a7a.gif|left|200px]]<br /><applet load="2a7a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2a7a, resolution 1.75&Aring;" />
'''On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength'''<br />


==Overview==
==On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength==
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.
<StructureSection load='2a7a' size='340' side='right'caption='[[2a7a]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2a7a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_cathartica Canavalia cathartica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7a OCA], [https://pdbe.org/2a7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7a RCSB], [https://www.ebi.ac.uk/pdbsum/2a7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CONA_CANCT CONA_CANCT] Glucose/D-mannose specific lectin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/2a7a_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a7a ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2A7A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_virosa Canavalia virosa] with MN, CA and XE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A7A OCA].
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16131760 16131760]
[[Category: Canavalia cathartica]]
[[Category: Canavalia virosa]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Mueller-Dieckmann C]]
[[Category: Mueller-Dieckmann, C.]]
[[Category: Panjikar S]]
[[Category: Panjikar, S.]]
[[Category: Tucker PA]]
[[Category: Tucker, P.A.]]
[[Category: Weiss MS]]
[[Category: Weiss, M.S.]]
[[Category: CA]]
[[Category: MN]]
[[Category: XE]]
[[Category: lectin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:57:33 2007''

Latest revision as of 09:11, 14 February 2024

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

2a7a, resolution 1.75Å

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