Literature DB >> 18540057

Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex.

Marco Túlio Ribeiro Gomes1, Raphael Dias Teixeira, Henrique de Assis Lopes Ribeiro, Andréia Pereira Turchetti, Caroline Furtado Junqueira, Míriam Tereza Paz Lopes, Carlos Edmundo Salas, Ronaldo Alves Pinto Nagem.   

Abstract

Cysteine proteinases from the latex of plants of the family Caricaceae are widely used industrially as well as in pharmaceutical preparations. In the present work, a 23 kDa cysteine proteinase from Carica candamarcensis latex (designated CMS1MS2) was purified for crystallization using three chromatography steps. The enzyme shows about fourfold higher activity than papain with BAPNA as substrate. Crystals suitable for X-ray diffraction experiments were obtained by the hanging-drop method in the presence of PEG and ammonium sulfate as precipitants. The crystals are monoclinic (space group P2(1)), with unit-cell parameters a = 53.26, b = 75.71, c = 53.23 A, beta = 96.81 degrees , and diffract X-rays to 1.8 A resolution.

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Year:  2008        PMID： 18540057      PMCID： PMC2496862          DOI： 10.1107/S174430910801172X

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  17 in total

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  2 in total

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  2 in total

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