1l0w
From Proteopedia
(New page: 200px<br /><applet load="1l0w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0w, resolution 2.01Å" /> '''Aspartyl-tRNA synthe...) |
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| - | [[Image:1l0w.jpg|left|200px]]<br /><applet load="1l0w" size=" | + | [[Image:1l0w.jpg|left|200px]]<br /><applet load="1l0w" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l0w, resolution 2.01Å" /> | caption="1l0w, resolution 2.01Å" /> | ||
'''Aspartyl-tRNA synthetase-1 from space-grown crystals'''<br /> | '''Aspartyl-tRNA synthetase-1 from space-grown crystals'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein crystallization under microgravity aims at benefiting from the | + | 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== | ==About this Structure== | ||
| - | 1L0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [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] Full crystallographic information is available from [http:// | + | 1L0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kirkland, N.]] | [[Category: Kirkland, N.]] | ||
[[Category: Lorber, B.]] | [[Category: Lorber, B.]] | ||
| - | [[Category: Ng, J | + | [[Category: Ng, J D.]] |
[[Category: Sauter, C.]] | [[Category: Sauter, C.]] | ||
[[Category: dimeric enzyme]] | [[Category: dimeric enzyme]] | ||
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[[Category: space-grown crystal]] | [[Category: space-grown crystal]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:03 2008'' |
Revision as of 11:40, 21 February 2008
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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. Active as Aspartate--tRNA ligase, with EC number 6.1.1.12 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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