Article (Scientific journals)
Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-binding DD-transpeptidase.
Englebert, S.; Charlier, Paulette; Fonze, E. et al.
1994In Journal of Molecular Biology, 241 (2), p. 295-7
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Keywords :
Bacterial Proteins; Carrier Proteins/chemistry/isolation & purification/metabolism; Crystallization; Crystallography, X-Ray; Hexosyltransferases; Mass Spectrometry; Muramoylpentapeptide Carboxypeptidase/chemistry/isolation & purification/metabolism; Penicillin-Binding Proteins; Penicillins/metabolism; Peptidyl Transferases; Streptomyces/enzymology
Abstract :
[en] The 262 amino acid residue long DD-transpeptidase/penicillin-binding protein of Streptomyces K15 has been crystallized at room temperature by using the hanging drop vapour diffusion technique. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell parameters a = 46.4 A, b = 54.1 A and c = 108.3 A. They contain one protein molecule per asymmetric unit and diffract to about 1.9 A. X-ray data have been collected to 2.0 A from a native crystal. The previously published amino acid sequence of the protein has been corrected at positions 71, 72, 113, 114 and 156.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Englebert, S.
Charlier, Paulette ;  Université de Liège - ULiège > Département des sciences de la vie > Cristallographie des macromolécules biologiques
Fonze, E.
To'th, Y.
Vermeire, M.
Van Beeumen, J.
Grandchamps, J.
Hoffmann, K.
Leyh-Bouille, M.
Nguyen-Distèche, Martine 
Ghuysen, Jean-Marie 
Language :
English
Title :
Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-binding DD-transpeptidase.
Publication date :
1994
Journal title :
Journal of Molecular Biology
ISSN :
0022-2836
eISSN :
1089-8638
Publisher :
Academic Press, London, United Kingdom
Volume :
241
Issue :
2
Pages :
295-7
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 28 November 2010

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