4pgo: Difference between revisions

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<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=4pgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgo RCSB], [http://www.ebi.ac.uk/pdbsum/4pgo PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.

Fast native-SAD phasing for routine macromolecular structure determination.,Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719<ref>PMID:25506719</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 7: / Line 7: @@
 <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=4pgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pgo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pgo RCSB], [http://www.ebi.ac.uk/pdbsum/4pgo PDBsum]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
+Fast native-SAD phasing for routine macromolecular structure determination.,Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719<ref>PMID:25506719</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>