Reference : Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sen...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/91673
Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus g
English
Dideberg, Otto [Université de Liège - ULiège > Insitut de Chimie > Laboratoire de Cristallographie > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > > Service de Microbiologie > > > >]
25-Apr-1979
Journal of Molecular Biology
Academic Press
129
4
677-679
Yes (verified by ORBi)
International
0022-2836
1089-8638
London
United Kingdom
[en] alanine ; crystallization ; dipeptides ; endopeptidases/isolation & purification ; kinetics ; streptomyces/*enzymology ; x-ray diffraction
[en] The DD-carboxypeptidase-endopeptidase of low penicillin sensitivity that is excreted by Streptomyces albus G has been crystallized from a polyethylene glycol (Mr 6000 to 7500) solution at pH 8.0. X-ray examination of the prismatic crystals shows that the space group is P21 with unit cell dimensions a = 51.1 Å, B = 49.7 Å, C = 38.7 Å, β = 100.6 ° and one molecule in the asymmetric unit. A crystal suspension made in 50 mM -Tris • HCl buffer (pH 8.0) supplemented with 5 mM-MgCl2 and 16% (w/v) polyethylene glycol exhibits enzyme activity on the substrate Ac2-L-Lys-D-Ala-D-Ala.
National Institutes of Health - NIH ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals
http://hdl.handle.net/2268/91673

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