1l0w: Difference between revisions
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'''Aspartyl-tRNA synthetase-1 from space-grown crystals''' | {{Structure | ||
|PDB= 1l0w |SIZE=350|CAPTION= <scene name='initialview01'>1l0w</scene>, resolution 2.01Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Aspartyl-tRNA synthetase-1 from space-grown crystals''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1L0W is a [ | 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== | ==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:// | 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: Aspartate--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Sauter, C.]] | [[Category: Sauter, C.]] | ||
[[Category: dimeric enzyme]] | [[Category: dimeric enzyme]] | ||
[[Category: flexible | [[Category: flexible domain]] | ||
[[Category: space-grown crystal]] | [[Category: space-grown crystal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:24:52 2008'' | ||
Revision as of 10:24, 20 March 2008
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| 1l0w, resolution 2.01Å | |||||||||||||
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| Activity: | Aspartate--tRNA ligase, with EC number 6.1.1.12 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Aspartyl-tRNA synthetase-1 from space-grown crystals
Overview
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.
About this Structure
1L0W is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from 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:11914489
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