Reference : Crystallization of a genetically engineered water-soluble primary penicillin target enzy...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/77981
Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae.
English
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
Buisson, G. [> > > >]
Dideberg, O. [> > > >]
Wierenga, J. [> > > >]
Keck, W. [> > > >]
Laible, G. [> > > >]
Hakenbeck, R. [> > > >]
1993
Journal of Molecular Biology
Academic Press
232
3
1007-9
Yes (verified by ORBi)
International
0022-2836
1089-8638
London
United Kingdom
[en] Bacterial Proteins ; Carrier Proteins/chemistry ; Crystallization ; Hexosyltransferases ; Muramoylpentapeptide Carboxypeptidase/chemistry ; Penicillin-Binding Proteins ; Peptidyl Transferases ; Protein Conformation ; Protein Engineering ; Recombinant Proteins/chemistry ; Solubility ; Streptococcus pneumoniae/enzymology ; Water ; X-Ray Diffraction
[en] A genetically engineered water-soluble derivative of PBP2x of Streptococcus pneumoniae has been produced, purified and crystallized in a form suitable for X-ray diffraction analysis. The best crystals have been grown at 15 degrees C, from solutions containing 8% polyethylene glycol 10,000 at pH values ranging from 3.9 to 6.0. These crystals diffract to a resolution of 3.5 A and have a space group P6(1)22 (or enantiomorph) with unit cell dimensions of a = b = 162.2 A, c = 171.8 A, alpha = beta = 90 degrees, gamma = 120 degrees. The molecular mass and cell dimensions suggest that there is one molecule of enzyme per asymmetric unit. The breakdown of a chromogenic cephalosporin derivative diffused into a crystal reveals clearly that the enzyme is active in the crystalline state.
http://hdl.handle.net/2268/77981
10.1006/jmbi.1993.1452

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