3wpl: Difference between revisions
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''' | ==SPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SEC== | ||
<StructureSection load='3wpl' size='340' side='right' caption='[[3wpl]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WPL FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PT4:PLATINUM+(IV)+ION'>PT4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wpj|3wpj]], [[3wu7|3wu7]], [[3wpk|3wpk]], [[3wu8|3wu8]], [[3wu9|3wu9]], [[3wua|3wua]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=3wpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wpl RCSB], [http://www.ebi.ac.uk/pdbsum/3wpl PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystal soaking is widely performed in biological crystallography. This paper reports time-resolved X-ray crystallographic and microtomographic analyses of tetragonal crystals of chicken egg-white lysozyme soaked in mother liquor containing potassium hexachloroplatinate. The microtomographic analysis showed that X-ray attenuation spread from the superficial layer of the crystal and then to the crystal core. The crystallographic analyses indicated that platinum sites can be classified into two groups from the temporal development of the electron densities. A soaking process consisting of binding-rate-driven and equilibrium-driven layers is proposed to describe these results. This study suggests that the composition of chemical and structural species resulting from the soaking process varies depending on the position in the crystal. | |||
Spatiotemporal development of soaked protein crystal.,Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871<ref>PMID:25043871</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Lysozyme]] | |||
[[Category: Mizutani, R.]] | |||
[[Category: Saiga, R.]] | |||
[[Category: Bacterial cell wall lysis]] | |||
[[Category: Hydrolase]] | |||
Revision as of 10:40, 30 July 2014
SPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SECSPATIOTEMPORAL DEVELOPMENT of SOAKED PROTEIN CRYSTAL; 2510 SEC
Structural highlights
Publication Abstract from PubMedCrystal soaking is widely performed in biological crystallography. This paper reports time-resolved X-ray crystallographic and microtomographic analyses of tetragonal crystals of chicken egg-white lysozyme soaked in mother liquor containing potassium hexachloroplatinate. The microtomographic analysis showed that X-ray attenuation spread from the superficial layer of the crystal and then to the crystal core. The crystallographic analyses indicated that platinum sites can be classified into two groups from the temporal development of the electron densities. A soaking process consisting of binding-rate-driven and equilibrium-driven layers is proposed to describe these results. This study suggests that the composition of chemical and structural species resulting from the soaking process varies depending on the position in the crystal. Spatiotemporal development of soaked protein crystal.,Mizutani R, Shimizu Y, Saiga R, Ueno G, Nakamura Y, Takeuchi A, Uesugi K, Suzuki Y Sci Rep. 2014 Jul 21;4:5731. doi: 10.1038/srep05731. PMID:25043871[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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