5uu9: Difference between revisions
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<StructureSection load='5uu9' size='340' side='right' caption='[[5uu9]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5uu9' size='340' side='right' caption='[[5uu9]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5uu9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UU9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5uu9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'bacillus_thermoproteolyticus' 'bacillus thermoproteolyticus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UU9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5un3|5un3]], [[5uu7|5uu7]], [[5uu8|5uu8]], [[5uua|5uua]], [[5uub|5uub]], [[5uuc|5uuc]], [[5uud|5uud]], [[5uue|5uue]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5un3|5un3]], [[5uu7|5uu7]], [[5uu8|5uu8]], [[5uua|5uua]], [[5uub|5uub]], [[5uuc|5uuc]], [[5uud|5uud]], [[5uue|5uue]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">npr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1427 'Bacillus thermoproteolyticus'])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </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=5uu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uu9 OCA], [http://pdbe.org/5uu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uu9 RCSB], [http://www.ebi.ac.uk/pdbsum/5uu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uu9 ProSAT]</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=5uu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uu9 OCA], [http://pdbe.org/5uu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uu9 RCSB], [http://www.ebi.ac.uk/pdbsum/5uu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uu9 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease. | [[http://www.uniprot.org/uniprot/THER_BACTH THER_BACTH]] Extracellular zinc metalloprotease. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling. | |||
The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.,Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):922-938. doi:, 10.1107/S2059798318008793. Epub 2018 Sep 5. PMID:30198901<ref>PMID:30198901</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5uu9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thermolysin|Thermolysin]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus thermoproteolyticus]] | |||
[[Category: Thermolysin]] | [[Category: Thermolysin]] | ||
[[Category: Juers, D H]] | [[Category: Juers, D H]] | ||
Revision as of 23:08, 19 September 2018
Tetragonal thermolysin cryocooled to 100 K with 40% xylose as cryoprotectantTetragonal thermolysin cryocooled to 100 K with 40% xylose as cryoprotectant
Structural highlights
Function[THER_BACTH] Extracellular zinc metalloprotease. Publication Abstract from PubMedCryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling. The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.,Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z Acta Crystallogr D Struct Biol. 2018 Sep 1;74(Pt 9):922-938. doi:, 10.1107/S2059798318008793. Epub 2018 Sep 5. PMID:30198901[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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