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Article

Crystallization and preliminary X-ray crystallographic study of the wild type and two mutants of the CP1 hydrolytic domain from Aquifex aeolicus leucyl-tRNA synthetase.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Oct 2005

Cura Vincent, Olieric Natacha, Guichard Alexandre, Wang En-Duo, Moras Dino, Eriani Gilbert, Cavarelli Jean

Abstract excerpt

The editing or hydrolytic CP1 domain of leucyl-tRNA synthetase (LeuRS) hydrolyses several misactivated amino acids. The CP1 domain of Aquifex aeolicus LeuRS was expressed, purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as precipitant. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.8, b = 98.4, c = 116.7 A. Crystals diffract to beyond...

Topics

Alanine
Bacteria
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Glutamic Acid
Hydrolysis
Leucine-tRNA Ligase
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Isoforms

Protein Structure, Tertiary

X-Ray Diffraction

Source

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Identifiers

PMID: 16511190
DOI: 10.1107/S1744309105028460
PMCID: PMC1991315

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