4zg3: Difference between revisions
New page: '''Unreleased structure''' The entry 4zg3 is ON HOLD Authors: Wagner, A., Duman, R., Henderson, K., Mykhaylyk, V. Description: Long-wavelength in vacuum molecular crystallography [[Cat... |
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==In-vacuum long-wavelength crystallography== | |||
<StructureSection load='4zg3' size='340' side='right'caption='[[4zg3]], [[Resolution|resolution]] 1.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZG3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=4zg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zg3 OCA], [https://pdbe.org/4zg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zg3 RCSB], [https://www.ebi.ac.uk/pdbsum/4zg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zg3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structure solution based on the weak anomalous signal from native (protein and DNA) crystals is increasingly being attempted as part of synchrotron experiments. Maximizing the measurable anomalous signal by collecting diffraction data at longer wavelengths presents a series of technical challenges caused by the increased absorption of X-rays and larger diffraction angles. A new beamline at Diamond Light Source has been built specifically for collecting data at wavelengths beyond the capability of other synchrotron macromolecular crystallography beamlines. Here, the theoretical considerations in support of the long-wavelength beamline are outlined and the in-vacuum design of the endstation is discussed, as well as other hardware features aimed at enhancing the accuracy of the diffraction data. The first commissioning results, representing the first in-vacuum protein structure solution, demonstrate the promising potential of the beamline. | |||
In-vacuum long-wavelength macromolecular crystallography.,Wagner A, Duman R, Henderson K, Mykhaylyk V Acta Crystallogr D Struct Biol. 2016 Mar 1;72(Pt 3):430-9. doi:, 10.1107/S2059798316001078. Epub 2016 Mar 1. PMID:26960130<ref>PMID:26960130</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4zg3" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thaumatococcus daniellii]] | |||
[[Category: Duman R]] | |||
[[Category: Henderson K]] | |||
[[Category: Mykhaylyk V]] | |||
[[Category: Wagner A]] | |||
Latest revision as of 10:26, 18 May 2023
In-vacuum long-wavelength crystallographyIn-vacuum long-wavelength crystallography
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedStructure solution based on the weak anomalous signal from native (protein and DNA) crystals is increasingly being attempted as part of synchrotron experiments. Maximizing the measurable anomalous signal by collecting diffraction data at longer wavelengths presents a series of technical challenges caused by the increased absorption of X-rays and larger diffraction angles. A new beamline at Diamond Light Source has been built specifically for collecting data at wavelengths beyond the capability of other synchrotron macromolecular crystallography beamlines. Here, the theoretical considerations in support of the long-wavelength beamline are outlined and the in-vacuum design of the endstation is discussed, as well as other hardware features aimed at enhancing the accuracy of the diffraction data. The first commissioning results, representing the first in-vacuum protein structure solution, demonstrate the promising potential of the beamline. In-vacuum long-wavelength macromolecular crystallography.,Wagner A, Duman R, Henderson K, Mykhaylyk V Acta Crystallogr D Struct Biol. 2016 Mar 1;72(Pt 3):430-9. doi:, 10.1107/S2059798316001078. Epub 2016 Mar 1. PMID:26960130[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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