1o81

==TRYPAREDOXIN II FROM C.FASCICULATA SOLVED BY SULPHUR PHASING==

<StructureSection load='1o81' size='340' side='right' caption='[[1o81]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1o81]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crithidia_fasciculata Crithidia fasciculata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O81 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O81 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o81 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o81 RCSB], [http://www.ebi.ac.uk/pdbsum/1o81 PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/1o81_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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== References ==

<references/>

[[Category: Hunter, W N.]]

[[Category: Leonard, G A.]]

[[Category: Micossi, E.]]

[[Category: Electron transport]]

[[Category: Tryparedoxin ii]]