4c3c: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c3c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3C FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
<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=4c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3c RCSB], [http://www.ebi.ac.uk/pdbsum/4c3c 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=4c3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3c RCSB], [http://www.ebi.ac.uk/pdbsum/4c3c PDBsum]</span></td></tr>
<table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy.
 
Time-resolved crystallography using the Hadamard transform.,Yorke BA, Beddard GS, Owen RL, Pearson AR Nat Methods. 2014 Nov;11(11):1131-4. doi: 10.1038/nmeth.3139. Epub 2014 Oct 5. PMID:25282611<ref>PMID:25282611</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Thaumatococcus daniellii]]
[[Category: Thaumatococcus daniellii]]
[[Category: Beddard, G S.]]
[[Category: Beddard, G S]]
[[Category: Owen, R L.]]
[[Category: Owen, R L]]
[[Category: Pearson, A R.]]
[[Category: Pearson, A R]]
[[Category: Yorke, B A.]]
[[Category: Yorke, B A]]
[[Category: Hatrx]]
[[Category: Hatrx]]
[[Category: Plant protein]]
[[Category: Plant protein]]
[[Category: Radiation damage]]
[[Category: Radiation damage]]
[[Category: Time-resolved crystallography]]
[[Category: Time-resolved crystallography]]