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. 2006 Mar 1;62(Pt 3):235-7.
doi: 10.1107/S174430910600371X. Epub 2006 Feb 10.

Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds

Benildo S Cavada  1 , Emmanuel S Marinho, Emmanuel P Souza, Raquel G Benevides, Plínio Delatorre, Luis A G Souza, Kyria S Nascimento, Alexandre H Sampaio, Frederico B M B Moreno, Joane K R Rustiguel, Fernanda Canduri, Walter F de Azevedo Jr, Henri Debray
Affiliations

Purification, partial characterization and preliminary X-ray diffraction analysis of a mannose-specific lectin from Cymbosema roseum seeds

Benildo S Cavada et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

A lectin from Cymbosema roseum seeds (CRL) was purified, characterized and crystallized. The best crystals grew in a month and were obtained by the vapour-diffusion method using a precipitant solution consisting of 0.1 M Tris-HCl pH 7.8, 8%(w/v) PEG 3350 and 0.2 M proline at a constant temperature of 293 K. A data set was collected to 1.77 A resolution at a synchrotron-radiation source. CRL crystals are orthorhombic, belonging to space group P2(1)2(1)2(1). Crystallographic refinement and full amino-acid sequence determination are in progress.

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Figures

Figure 1
Figure 1
(a) Crystal and (b) diffraction pattern of C. roseum lectin.
Figure 2
Figure 2
Affinity chromatography and SDS–PAGE of the purified C. roseum lectin (CRL). (a) Sepharose-4B-mannose chromatography. (b) SDS–PAGE showing protein markers (left) and a purified CRL band (right). The molecular-weight markers are bovine serum albumin (67 kDa), chymotrypsinogen (25 kDa) and lysozyme (14 kDa). The gel was Coomassie blue stained.
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