1L0W

Aspartyl-tRNA synthetase-1 from space-grown crystals

Summary for 1L0W

• Entry DOI: 10.2210/pdb1l0w/pdb
• Descriptor: Aspartyl-tRNA synthetase (2 entities in total)
• Functional Keywords: space-grown crystal, dimeric enzyme, flexible domains, ligase
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P36419
• Total number of polymer chains: 2
• Total formula weight: 132249.55

Authors

Ng, J.D.,Sauter, C.,Lorber, B.,Kirkland, N.,Arnez, J.,Giege, R. (deposition date: 2002-02-14, release date: 2002-03-20, Last modification date: 2024-02-14)

Primary citation

Ng, J.D.,Sauter, C.,Lorber, B.,Kirkland, N.,Arnez, J.,Giege, R.
Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination.
Acta Crystallogr.,Sect.D, 58:645-652, 2002

PubMed Abstract: 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.

PubMed: 11914489
DOI: 10.1107/S0907444902003177

Experimental method

X-RAY DIFFRACTION (2.01 Å)