Reference : Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-bindin...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/77973
Crystallization and X-ray diffraction study of the Streptomyces K15 penicillin-binding DD-transpeptidase.
English
Englebert, S. [> > > >]
Charlier, Paulette mailto [Université de Liège - ULg > 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-Disteche, M. [> > > >]
1994
Journal of Molecular Biology
Academic Press
241
2
295-7
Yes (verified by ORBi)
International
0022-2836
1089-8638
London
United Kingdom
[en] 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
[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.
http://hdl.handle.net/2268/77973

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