1o6j: Difference between revisions

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<StructureSection load='1o6j' size='340' side='right'caption='[[1o6j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='1o6j' size='340' side='right'caption='[[1o6j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1o6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6J FirstGlance]. <br>
<table><tr><td colspan='2'>[[1o6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6J FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fg4|1fg4]], [[1i5g|1i5g]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</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=1o6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6j OCA], [https://pdbe.org/1o6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6j RCSB], [https://www.ebi.ac.uk/pdbsum/1o6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6j ProSAT]</span></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=1o6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6j OCA], [https://pdbe.org/1o6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6j RCSB], [https://www.ebi.ac.uk/pdbsum/1o6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O77093_CRIFA O77093_CRIFA]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1o6j ConSurf].
</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=1o6j ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The de novo phasing of the structures of two crystal forms of tryparedoxin II from Crithidia fasciculata has been carried out using single-wavelength anomalous diffraction techniques exploiting only the small anomalous signal from the S atoms intrinsic to the native protein. Data were collected at 1.77 A wavelength, where the Bijvoet ratio is approximately 1.2%. Data collected to d(min) = 2.5 A from a crystal of form I, which has a diffraction limit of d(min) = 1.5 A and a solvent content of approximately 46%, produced readily interpretable electron-density maps. When these phases were extended to the resolution limit of the crystals, almost the entire model could be traced automatically. Crystals of form II have a much higher solvent content, approximately 72%, and a much lower diffraction limit than form I and at 1.77 A wavelength yielded data only to d(min) = 2.7 A. Despite the medium resolution of the data for this crystal form, it was possible both to determine the heavy-atom partial structure and then use it to produce, still at d(min) = 2.7 A, an excellent quality interpretable electron-density map. This was then improved by phase extension to the d(min) = 2.35 A diffraction limits of a different crystal for which data were collected on a more intense beamline. The success of this latter structure solution markedly increases the potential use in macromolecular crystal structure determination of the anomalous signal available from S atoms that occur naturally in proteins and, as is discussed, has significant implications for structure determination in the high-throughput era.
De novo phasing of two crystal forms of tryparedoxin II using the anomalous scattering from S atoms: a combination of small signal and medium resolution reveals this to be a general tool for solving protein crystal structures.,Micossi E, Hunter WN, Leonard GA Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):21-8. Epub 2001 Dec, 21. PMID:11752776<ref>PMID:11752776</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1o6j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Crifa]]
[[Category: Crithidia fasciculata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hunter, W N]]
[[Category: Hunter WN]]
[[Category: Leonard, G A]]
[[Category: Leonard GA]]
[[Category: Micossi, E]]
[[Category: Micossi E]]
[[Category: Electron transport]]
[[Category: S-sad]]
[[Category: Sad]]
[[Category: Sulphur phasing]]
[[Category: Tryparedoxin ii]]

Revision as of 08:55, 10 April 2024

Tryparedoxin II from C.fasciculata solved by sulphur phasing

1o6j, resolution 2.35Å

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