par Haesaerts, Sarah;Rodriguez Buitrago, John Alexander ;Loris, Remy;Volant-Baeyens, Danielle ;Azarkan, Mohamed
Référence Acta Crystallographica Section F:Structural Biology Communications, 71, page (459-465)
Publication Publié, 2015-04
Référence Acta Crystallographica Section F:Structural Biology Communications, 71, page (459-465)
Publication Publié, 2015-04
Article révisé par les pairs
Résumé : | The latex of the common fig (Ficus carica) contains a mixture of at least five cysteine proteases commonly known as ficins (EC 3.4.22.3). Four of these proteases were purified to homogeneity and crystals were obtained in a variety of conditions. The four ficin (iso)forms appear in ten different crystal forms. All diffracted to better than 2.10 Å resolution and for each form at least one crystal form diffracted to 1.60 Å resolution or higher. Ficin (iso)forms B and C share a common crystal form, suggesting close sequence and structural similarity. The latter diffracted to a resolution of 1.20 Å and belonged to space group P3121 or P3221, with unit-cell parameters a = b = 88.9, c = 55.9 Å. |