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1l0w
From Proteopedia
(Difference between revisions)
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<StructureSection load='1l0w' size='340' side='right'caption='[[1l0w]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='1l0w' size='340' side='right'caption='[[1l0w]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1l0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1l0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0W 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]] 2.01Å</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=1l0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0w OCA], [https://pdbe.org/1l0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0w RCSB], [https://www.ebi.ac.uk/pdbsum/1l0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0w 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=1l0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0w OCA], [https://pdbe.org/1l0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0w RCSB], [https://www.ebi.ac.uk/pdbsum/1l0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SYD_THETH SYD_THETH] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0w ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0w ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Protein crystallization under microgravity aims at benefiting from the quasi-absence of convection and sedimentation to favor well ordered crystal nucleation and growth. The dimeric multidomain enzyme aspartyl-tRNA synthetase from Thermus thermophilus has been crystallized within dialysis reactors of the Advanced Protein Crystallization Facility in the laboratory on earth and under microgravity aboard the US Space Shuttle. A strictly comparative crystallographic analysis reveals that the crystals grown in space are superior in every respect to control crystals prepared in otherwise identical conditions on earth. They diffract X-rays more intensely and have a lower mosaicity, facilitating the process of protein structure determination. Indeed, the electron-density map calculated from diffraction data of space-grown crystals contains considerably more detail. The resulting three-dimensional structure model at 2.0 A resolution is more accurate than that produced in parallel using the data originating from earth-grown crystals. The major differences between the structures, including the better defined amino-acid side chains and the higher order of bound water molecules, are emphasized. | ||
| - | |||
| - | Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination.,Ng JD, Sauter C, Lorber B, Kirkland N, Arnez J, Giege R Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):645-52. Epub 2002, Mar 22. PMID:11914489<ref>PMID:11914489</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1l0w" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | ||
| - | [[Category: Aspartate--tRNA ligase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arnez | + | [[Category: Thermus thermophilus]] |
| - | [[Category: Giege | + | [[Category: Arnez J]] |
| - | [[Category: Kirkland | + | [[Category: Giege R]] |
| - | [[Category: Lorber | + | [[Category: Kirkland N]] |
| - | [[Category: Ng | + | [[Category: Lorber B]] |
| - | [[Category: Sauter | + | [[Category: Ng JD]] |
| - | + | [[Category: Sauter C]] | |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Aspartyl-tRNA synthetase-1 from space-grown crystals
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Categories: Large Structures | Thermus thermophilus | Arnez J | Giege R | Kirkland N | Lorber B | Ng JD | Sauter C

