Open AccessCrystallization and preliminary X‐ray diffraction studies of the cysteine protease ervatamin A from Ervatamia coronaria
Author(s) -
Chakraborty Sibani,
Biswas Sampa,
Chakrabarti Chandana,
Dattagupta Jiban K.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910501657x
Subject(s) - proteases , papain , crystallization , protease , cysteine , crystallography , cysteine protease , chemistry , solvent , molecule , x ray crystallography , molecular replacement , stereochemistry , diffraction , enzyme , biochemistry , organic chemistry , physics , optics
The ervatamins are highly stable cysteine proteases that are present in the latex of the medicinal plant Ervatamia coronaria and belong to the papain family, members of which share similar amino‐acid sequences and also a similar fold comprising two domains. Ervatamin A from this family, a highly active protease compared with others from the same source, has been purified to homogeneity by ion‐exchange chromatography and crystallized by the vapour‐diffusion method. Needle‐shaped crystals of ervatamin A diffract to 2.1 Å resolution and belong to space group C 222 1 , with unit‐cell parameters a = 31.10, b = 144.17, c = 108.61 Å. The solvent content using an ervatamin A molecular weight of 27.6 kDa is 43.9%, with a V M value of 2.19 Å 3 Da −1 assuming one protein molecule in the asymmetric unit. A molecular‐replacement solution has been found using the structure of ervatamin C as a search model.