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

Marco Túlio Ribeiro Gomes; 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

doi:10.1107/S174430910801172X

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

Marco Túlio Ribeiro Gomes
, 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

Biosciences

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	492-494
Number of pages	3
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	64
Issue number	Pt 6
DOIs	https://doi.org/10.1107/S174430910801172X
Publication status	Published - 1 Jun 2008

Keywords

Crystallography
X-Ray
Carica
Cysteine Endopeptidases
Latex
Plant Proteins
Benzoylarginine Nitroanilide
Chromogenic Compounds
Molecular Weight
X-Ray Diffraction

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10.1107/S174430910801172X

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Gomes, M. T. R., Teixeira, R. D., Ribeiro, H. D. A. L., Turchetti, A. P., Junqueira, C. F., Lopes, M. T. P., Salas, C. E., & Nagem, R. A. P. (2008). Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 64(Pt 6), 492-494. https://doi.org/10.1107/S174430910801172X

@article{a0d02115a59c4d6095c9dfc59e85a67c,

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

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.",

keywords = "Crystallography, X-Ray, Carica, Cysteine Endopeptidases, Latex, Plant Proteins, Benzoylarginine Nitroanilide, Chromogenic Compounds, Molecular Weight, X-Ray Diffraction",

author = "Gomes, \{Marco T{\'u}lio Ribeiro\} and Teixeira, \{Raphael Dias\} and Ribeiro, \{Henrique de Assis Lopes\} and Turchetti, \{Andr{\'e}ia Pereira\} and Junqueira, \{Caroline Furtado\} and Lopes, \{M{\'i}riam Tereza Paz\} and Salas, \{Carlos Edmundo\} and Nagem, \{Ronaldo Alves Pinto\}",

year = "2008",

month = jun,

day = "1",

doi = "10.1107/S174430910801172X",

language = "English",

volume = "64",

pages = "492--494",

journal = "Acta Crystallographica Section F Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "International Union of Crystallography",

number = "Pt 6",

}

Gomes, MTR, Teixeira, RD, Ribeiro, HDAL, Turchetti, AP, Junqueira, CF, Lopes, MTP, Salas, CE & Nagem, RAP 2008, 'Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex', Acta Crystallographica Section F Structural Biology and Crystallization Communications, vol. 64, no. Pt 6, pp. 492-494. https://doi.org/10.1107/S174430910801172X

Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex. / Gomes, Marco Túlio Ribeiro; Teixeira, Raphael Dias; Ribeiro, Henrique de Assis Lopes et al.
In: Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 64, No. Pt 6, 01.06.2008, p. 492-494.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray analysis of CMS1MS2: a cysteine proteinase from Carica candamarcensis latex

AU - Gomes, Marco Túlio Ribeiro

AU - Teixeira, Raphael Dias

AU - Ribeiro, Henrique de Assis Lopes

AU - Turchetti, Andréia Pereira

AU - Junqueira, Caroline Furtado

AU - Lopes, Míriam Tereza Paz

AU - Salas, Carlos Edmundo

AU - Nagem, Ronaldo Alves Pinto

PY - 2008/6/1

Y1 - 2008/6/1

N2 - 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.

AB - 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.

KW - Crystallography

KW - X-Ray

KW - Carica

KW - Cysteine Endopeptidases

KW - Latex

KW - Plant Proteins

KW - Benzoylarginine Nitroanilide

KW - Chromogenic Compounds

KW - Molecular Weight

KW - X-Ray Diffraction

U2 - 10.1107/S174430910801172X

DO - 10.1107/S174430910801172X

M3 - Article

SN - 1744-3091

VL - 64

SP - 492

EP - 494

JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F Structural Biology and Crystallization Communications

IS - Pt 6

ER -

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

Abstract

Keywords

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