3n0b: Difference between revisions
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<StructureSection load='3n0b' size='340' side='right'caption='[[3n0b]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3n0b' size='340' side='right'caption='[[3n0b]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3n0b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3n0b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N0B FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n0b OCA], [https://pdbe.org/3n0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n0b RCSB], [https://www.ebi.ac.uk/pdbsum/3n0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n0b ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n0b OCA], [https://pdbe.org/3n0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n0b RCSB], [https://www.ebi.ac.uk/pdbsum/3n0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n0b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Mathews II]] | ||
Latest revision as of 12:06, 6 September 2023
TM0449 mutant crystals grown in loops/micromountsTM0449 mutant crystals grown in loops/micromounts
Structural highlights
FunctionTHYX_THEMA Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. Publication Abstract from PubMedProtein crystals are usually grown in hanging or sitting drops and generally get transferred to a loop or micromount for cryocooling and data collection. This paper describes a method for growing crystals on cryoloops for easier manipulation of the crystals for data collection. This study also investigates the steps for the automation of this process and describes the design of a new tray for the method. The diffraction patterns and the structures of three proteins grown by both the new method and the conventional hanging-drop method are compared. The new setup is optimized for the automation of the crystal mounting process. Researchers could prepare nanolitre drops under ordinary laboratory conditions by growing the crystals directly in loops or micromounts. As has been pointed out before, higher levels of supersaturation can be obtained in very small volumes, and the new method may help in the exploration of additional crystallization conditions. Diffraction study of protein crystals grown in cryoloops and micromounts.,Berger MA, Decker JH, Mathews II J Appl Crystallogr. 2010 Dec 1;43(Pt 6):1513-1518. Epub 2010 Oct 20. PMID:22477781[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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