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Preliminary Crystallographic Analysis of a Cruciferin Protein from Seeds of Moringa oleifera

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Abstract

A 55 kDa cruciferin protein has been purified and characterized from seeds of Moringa oleifera plant. Protein blast of N-terminal amino-acid sequence showed 60 % sequence similarity with cruciferin from Brassica napus. The M. oleifera protein has been crystallized applying the sitting drop method using 5 % polyethylene glycol 8,000, 38.5 % 3-methyl-1,5-pentanediol and 0.1 M sodium cacodylate pH 6.5. The crystals belonged to the P6322 hexagonal space group with cell dimensions, a = b = 98.4, c = 274.3 Å. Initial diffraction data have been collected to a resolution of 6 Å.

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Abbreviations

PEG:

Polyethylene glycol

MPD:

3-Methyl-1,5-pentanediol

MO:

Moringa oleifera

DESY:

Deutsches Elektronen Synchrotron

SDS-PAGE:

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis

DLS:

Dynamic light scattering

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Acknowledgments

The work was supported by Higher Education Commission (HEC), Pakistan and Deutscher Akademischer Austausch Dienst (DAAD), Germany under the collaborative project “Ph.D scholarships for Engineering & Sciences in Germany’’ as a part of Human Resource Development (HRD) plan of Pakistan government.

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Correspondence to Ahmed Akrem.

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Akrem, A., Yousef, N., Begum, A. et al. Preliminary Crystallographic Analysis of a Cruciferin Protein from Seeds of Moringa oleifera . Protein J 33, 253–257 (2014). https://doi.org/10.1007/s10930-014-9558-x

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