Premium
Crystallization and preliminary X‐ray analysis of four cysteine proteases from Ficus carica latex
Author(s) -
Haesaerts Sarah,
Rodriguez Buitrago John Alexander,
Loris Remy,
BaeyensVolant Danielle,
Azarkan Mohamed
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15005014
Subject(s) - ficus , carica , proteases , crystallization , botany , chemistry , biology , biochemistry , enzyme , organic chemistry
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 P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 88.9, c = 55.9 Å.