Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.

TitleCrystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.
Publication TypeJournal Article
Year of Publication2015
AuthorsHaesaerts, S., J. Alexander Buitrago, R. Loris, D. Baeyens-Volant, and M. Azarkan
JournalActa Crystallogr F Struct Biol Commun
Volume71
IssuePt 4
Pagination459-65
Date Published2015 Apr
ISSN2053-230X
KeywordsCrystallization, Crystallography, X-Ray, Cysteine Proteases, Ficus, Latex, Plant Proteins
Abstract

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.

DOI10.1107/S2053230X15005014
Alternate JournalActa Crystallogr F Struct Biol Commun
PubMed ID25849510
PubMed Central IDPMC4388184
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