|Title||Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.|
|Publication Type||Journal Article|
|Year of Publication||2015|
|Authors||Haesaerts, S., J. Alexander Buitrago, R. Loris, D. Baeyens-Volant, and M. Azarkan|
|Journal||Acta Crystallogr F Struct Biol Commun|
|Date Published||2015 Apr|
|Keywords||Crystallization, Crystallography, X-Ray, Cysteine Proteases, Ficus, Latex, Plant Proteins|
The latex of the common fig (Ficus carica) contains a mixture of at least five cysteine proteases commonly known as ficins (EC 126.96.36.199). 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.
|Alternate Journal||Acta Crystallogr F Struct Biol Commun|
|PubMed Central ID||PMC4388184|
Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.