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Purification, crystallization and preliminary X-ray analysis of mexicain

AuthorsOliver-Salvador, M. C.; González-Ramírez, L. A.; Gavira Gallardo, J. A. ; Soriano-García, M.; García Ruiz, Juan Manuel
Cysteine proteases
Issue DateNov-2004
PublisherInternational Union of Crystallography
CitationBiological Crystallography 60(11): 2058-2060 (2004
AbstractMexicain is a 23.7 kDa papain-like cysteine protease from the tropical plant Jacaratia mexicana. Extracted as a mix of proteases from the latex of the fruit, mexicain is isolated after cation-exchange chromatography as the most abundant product. The purified product inhibited with E-64 was crystallized by sitting-drop vapour diffusion in the presence of ethanolamine. Cryoprotected crystals diffracted X-rays from a home source to 1.98 Å and belong to the monoclinic space group P21, with unit-cell parameters a = 57.36, b = 90.45, c = 80.39 Å, [beta] = 92.64°. The asymmetric unit contains four molecules of mexicain, with a corresponding crystal volume per protein weight (VM) of 2.24 Å3 Da-1 and a solvent content of 45% by volume. A molecular-replacement model has been determined and refinement is in progress
Description3 pages, 1 table, 2 figures.
Publisher version (URL)http://dx.doi.org/10.1107/S0907444904021638
Appears in Collections:(IACT) Artículos
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