Re-designed N-terminus enhances expression, solubility and crystallizability of mitochondrial protein

Protein Engineering, Design and Selection

Volumn 25, Issue 9, 2012, Pages 473-481

  Gaudry, Agnès ^a   Lorber, Bernard ^a   Neuenfeldt, Anne ^a,b   Sauter, Claude ^a   Florentz, Catherine ^a   Sissler, Marie ^a  

^a UNIVERSITÉ DE STRASBOURG   (France)

^b CYANO BIOTECH GMBH   (Germany)

Author keywords

adenylate analogs; crystallization; human mitochondrial aminoacyl tRNA synthetase; protein engineering; solubility

Indexed keywords

ADENYLATE; CLEAVAGE SITES; CRYSTALLIZABILITY; CRYSTALLOGRAPHIC STUDIES; CYTOSOLS; KEY ENZYMES; MATURE PROTEINS; MITOCHONDRIAL PROTEIN; MONODISPERSE; N-TERMINALS; NATURAL AMINO ACIDS; NUCLEAR GENOMES; PROKARYOTIC SYSTEM; PROTEIN ENGINEERING; STRUCTURE DETERMINATION; SYNTHETASES;

AMINO ACIDS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYMES; GENETIC ENGINEERING; PROTEINS; RHENIUM;

SOLUBILITY;

ADENOSINE DERIVATIVE; ASPARTATE TRANSFER RNA LIGASE; MITOCHONDRIAL PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME CONFORMATION; MITOCHONDRIAL TARGETING SIGNAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SOLUBILITY;

AMINO ACID SEQUENCE; ASPARTATE-TRNA LIGASE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SOLUBILITY;

PROKARYOTA;

EID: 84865713635     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs046     Document Type: Article

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