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[[Image:1l0w.jpg|left|200px]]


{{Structure
==Aspartyl-tRNA synthetase-1 from space-grown crystals==
|PDB= 1l0w |SIZE=350|CAPTION= <scene name='initialview01'>1l0w</scene>, resolution 2.01&Aring;
<StructureSection load='1l0w' size='340' side='right'caption='[[1l0w]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate--tRNA_ligase Aspartate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.12 6.1.1.12] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
|GENE=
<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>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0w OCA], [http://www.ebi.ac.uk/pdbsum/1l0w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l0w RCSB]</span>
[https://www.uniprot.org/uniprot/SYD_THETH SYD_THETH]
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l0w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''Aspartyl-tRNA synthetase-1 from space-grown crystals'''
==See Also==
 
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1L0W is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11914489 11914489]
[[Category: Aspartate--tRNA ligase]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Arnez, J.]]
[[Category: Arnez J]]
[[Category: Giege, R.]]
[[Category: Giege R]]
[[Category: Kirkland, N.]]
[[Category: Kirkland N]]
[[Category: Lorber, B.]]
[[Category: Lorber B]]
[[Category: Ng, J D.]]
[[Category: Ng JD]]
[[Category: Sauter, C.]]
[[Category: Sauter C]]
[[Category: dimeric enzyme]]
[[Category: flexible domain]]
[[Category: space-grown crystal]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:25 2008''

Latest revision as of 07:29, 14 February 2024

Aspartyl-tRNA synthetase-1 from space-grown crystals

1l0w, resolution 2.01Å

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