2a7i

From Proteopedia

(Difference between revisions)

Revision as of 14:37, 17 November 2021

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

Structural highlights

2a7i is a 1 chain structure with sequence from Thaumatococcus daniellii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Complete and highly redundant data sets were collected at different wavelengths between 0.80 and 2.65 A for a total of ten different protein and DNA model systems. The magnitude of the anomalous signal-to-noise ratio as assessed by the quotient R(anom)/R(r.i.m.) was found to be influenced by the data-collection wavelength and the nature of the anomalously scattering substructure. By utilizing simple empirical correlations, for instance between the estimated deltaF/F and the expected R(anom) or the data-collection wavelength and the expected R(r.i.m.), the wavelength at which the highest anomalous signal-to-noise ratio can be expected could be estimated even before the experiment. Almost independent of the nature of the anomalously scattering substructure and provided that no elemental X-ray absorption edge is nearby, this optimal wavelength is 2.1 A.

On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength.,Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mueller-Dieckmann C, Panjikar S, Tucker PA, Weiss MS. On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength. Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1263-72. Epub 2005, Aug 16. PMID:16131760 doi:http://dx.doi.org/10.1107/S0907444905021475

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a7i"

@@ Line 3: / Line 3: @@
 <StructureSection load='2a7i' size='340' side='right'caption='[[2a7i]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2a7i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A7I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2a7i]] 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=2A7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A7I FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7i OCA], [http://pdbe.org/2a7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a7i RCSB], [http://www.ebi.ac.uk/pdbsum/2a7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7i 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=2a7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7i OCA], [https://pdbe.org/2a7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a7i RCSB], [https://www.ebi.ac.uk/pdbsum/2a7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a7i ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2a7i

From Proteopedia

Revision as of 14:37, 17 November 2021

On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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