1l0w
From Proteopedia
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| , resolution 2.01Å | |||||||
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| Activity: | Aspartate--tRNA ligase, with EC number 6.1.1.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:56:25 2008
