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Titolo:
LARGE-SCALE PREPARATION, PURIFICATION, AND CRYSTALLIZATION OF UDP-N-ACETYLURAMOYL-L-ALANINE - D-GLUTAMATE LIGASE FROM ESCHERICHIA-COLI
Autore:
AUGER G; MARTIN L; BERTRAND J; FERRARI P; FANCHON E; VAGANAY S; PETILLOT Y; VANHEIJENOORT J; BLANOT D; DIDEBERG O;
Indirizzi:
CNRS,CEA,INST BIOL STRUCT JEAN PIERRE EBEL,LAB CRISTALLOG MACROMOL,41AVE MARTYRS F-38027 GRENOBLE 01 FRANCE CNRS,CEA,INST BIOL STRUCT JEAN PIERRE EBEL,LAB CRISTALLOG MACROMOL F-38027 GRENOBLE 01 FRANCE UNIV PARIS 11,CNRS,UNITE RECH ASSOCIEE 1131 ORSAY FRANCE CNRS,CEA,INST BIOL STRUCT JEAN PIERRE EBEL,LAB SPECTROMETRIE MASSE PROT F-38027 GRENOBLE 01 FRANCE
Titolo Testata:
Protein expression and purification
fascicolo: 1, volume: 13, anno: 1998,
pagine: 23 - 29
SICI:
1046-5928(1998)13:1<23:LPPACO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID-ADDING ENZYME; MASS-SPECTROMETRY; PEPTIDOGLYCAN BIOSYNTHESIS; NUCLEOTIDE-SEQUENCE; ACETYLMURAMIC ACID; OVER-PRODUCTION; CELL-WALL; MURD; GENE; INHIBITORS;
Keywords:
DRUG DESIGN; OVERPRODUCTION; PEPTIDOGLYCAN; SELENOMETHIONINE; X-RAY CRYSTALLOGRAPHY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
G. Auger et al., "LARGE-SCALE PREPARATION, PURIFICATION, AND CRYSTALLIZATION OF UDP-N-ACETYLURAMOYL-L-ALANINE - D-GLUTAMATE LIGASE FROM ESCHERICHIA-COLI", Protein expression and purification, 13(1), 1998, pp. 23-29

Abstract

The UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli, an enzyme involved in the biosynthesis of the bacterial peptidoglycan monomer unit, was overproduced and purified to homogeneity on a large scale, yielding 4 mg of protein per liter of bacterial culture. Crystals of the complex with the substrate UDP-MurNAc-L-Ala were grown by the hanging drop method using ammonium sulfate as the precipitant. They are tetragonal with cell dimensions a = b = 65.5 Angstrom and c = 134.59 Angstrom, space group P4(1) or P4(3), and contain one monomer of 46,842 Da in the asymmetric unit. In order to use the multiple-wavelength anomalous diffraction method for phasing, a selenomethioninederivative of the protein has also been overproduced,purified, and crystallized. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 10:59:05