4axt: Difference between revisions
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==CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME FROM | ==CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME FROM AN AUTO HARVESTED CRYSTAL, Control Experiment== | ||
<StructureSection load='4axt' size='340' side='right' caption='[[4axt]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='4axt' size='340' side='right'caption='[[4axt]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4axt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4axt]] 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=4AXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AXT FirstGlance]. <br> | ||
</td></tr><tr id='activity'><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> | </td></tr><tr id='activity'><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 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=4axt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4axt OCA], [http://pdbe.org/4axt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4axt RCSB], [http://www.ebi.ac.uk/pdbsum/4axt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4axt 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=4axt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4axt OCA], [http://pdbe.org/4axt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4axt RCSB], [http://www.ebi.ac.uk/pdbsum/4axt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4axt ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Cipriani, F]] | [[Category: Cipriani, F]] | ||
Revision as of 12:30, 6 March 2019
CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME FROM AN AUTO HARVESTED CRYSTAL, Control ExperimentCRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME FROM AN AUTO HARVESTED CRYSTAL, Control Experiment
Structural highlights
Function[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] Publication Abstract from PubMedThe use of automated systems for crystallization and X-ray data collection is now widespread. However, these two steps are separated by the need to transfer crystals from crystallization supports to X-ray data-collection supports, which is a difficult manual operation. Here, a new approach is proposed called CrystalDirect (CD) which enables full automation of the crystal-harvesting process. In this approach, crystals are grown on ultrathin films in a newly designed vapour-diffusion crystallization plate and are recovered by excision of the film through laser-induced photoablation. The film pieces containing crystals are then directly attached to a pin for X-ray data collection. This new method eliminates the delicate step of `crystal fishing', thereby enabling full automation of the crystal-mounting process. Additional advantages of this approach include the absence of mechanical stress and that it facilitates handling of microcrystals. The CD crystallization plates are also suitable for in situ crystal screening with minimal X-ray background. This method could enable the operational integration of highly automated crystallization and data-collection facilities, minimizing the delay between crystal identification and diffraction measurements. It can also contribute significantly to the advancement of challenging projects that require the systematic testing of large numbers of crystals. CrystalDirect: a new method for automated crystal harvesting based on laser-induced photoablation of thin films.,Cipriani F, Rower M, Landret C, Zander U, Felisaz F, Marquez JA Acta Crystallogr D Biol Crystallogr. 2012 Oct;68(Pt 10):1393-9. Epub 2012 Sep 18. PMID:22993093[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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