par Oudjama, Yamina;Durbecq, Virginie ;Sainz, Germaine;Clantin, Bernard ;Tricot, Catherine ;Stalon, Victor ;Villeret, Vincent ;Droogmans, Louis
Référence Acta crystallographica. Section D, Biological crystallography, 57, 2, page (287-288)
Publication Publié, 2001-02
Référence Acta crystallographica. Section D, Biological crystallography, 57, 2, page (287-288)
Publication Publié, 2001-02
Article révisé par les pairs
Résumé : | Escherichia coli isopentenyl diphosphate isomerase, an enzyme catalyzing a key step in isoprenoid biosynthesis, has been produced in selenomethionyl form. The protein was purified and crystallized by the hanging-drop vapour-diffusion method. Crystals display trigonal symmetry, with unit-cell parameters a = b = 71.3, c = 61.7 A, and diffract to 1.45 A resolution. |