1l0w

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{{STRUCTURE_1l0w| PDB=1l0w | SCENE= }}
{{STRUCTURE_1l0w| PDB=1l0w | SCENE= }}
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'''Aspartyl-tRNA synthetase-1 from space-grown crystals'''
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===Aspartyl-tRNA synthetase-1 from space-grown crystals===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Flexible domain]]
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[[Category: Space-grown crystal]]
[[Category: Space-grown crystal]]
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Revision as of 08:27, 2 July 2008

Image:1l0w.png

Template:STRUCTURE 1l0w

Aspartyl-tRNA synthetase-1 from space-grown crystals

Template:ABSTRACT PUBMED 11914489

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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