par Marcq, S.;Diaz-Ruano, A.;Charlier, Paulette;Dideberg, Otto;Tricot, Catherine
;Pierard, André
;Stalon, Victor 
Référence Journal of Molecular Biology, 220, 1, page (9-12)
Publication Publié, 1991



Référence Journal of Molecular Biology, 220, 1, page (9-12)
Publication Publié, 1991
Article révisé par les pairs
Résumé : | The catabolic ornithine carbamoyltransferase (EC 2.1.3.3) from Pseudomonas aeruginosa, that shows allosteric behaviour, and a mutant version of this enzyme has been crystallized in several different crystal forms. All of these have been characterized by X-ray diffraction methods. A 4.5 Å resolution data set has been collected on a triclinic crystal. Analysis of the data using the self-rotation function shows that 12 monomers associate to form a particle with cubic 23 point group symmetry. |