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Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera

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Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera. / Akrem, Ahmed; Yousef, Nasser; Begum, Afshan; Negm, Amr; Meyer, Arne; Perbandt, Markus; Buck, Friedrich; Betzel, Christian.

in: PROTEIN J, Jahrgang 33, Nr. 3, 01.06.2014, S. 253-7.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Akrem, A, Yousef, N, Begum, A, Negm, A, Meyer, A, Perbandt, M, Buck, F & Betzel, C 2014, 'Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera', PROTEIN J, Jg. 33, Nr. 3, S. 253-7. https://doi.org/10.1007/s10930-014-9558-x

APA

Akrem, A., Yousef, N., Begum, A., Negm, A., Meyer, A., Perbandt, M., Buck, F., & Betzel, C. (2014). Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera. PROTEIN J, 33(3), 253-7. https://doi.org/10.1007/s10930-014-9558-x

Vancouver

Akrem A, Yousef N, Begum A, Negm A, Meyer A, Perbandt M et al. Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera. PROTEIN J. 2014 Jun 1;33(3):253-7. https://doi.org/10.1007/s10930-014-9558-x

Bibtex

@article{9f8cef9f31f44944aa0e331eac925e47,
title = "Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera",
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 {\AA}. Initial diffraction data have been collected to a resolution of 6 {\AA}.",
author = "Ahmed Akrem and Nasser Yousef and Afshan Begum and Amr Negm and Arne Meyer and Markus Perbandt and Friedrich Buck and Christian Betzel",
year = "2014",
month = jun,
day = "1",
doi = "10.1007/s10930-014-9558-x",
language = "English",
volume = "33",
pages = "253--7",
journal = "PROTEIN J",
issn = "1572-3887",
publisher = "Springer New York",
number = "3",

}

RIS

TY - JOUR

T1 - Preliminary crystallographic analysis of a cruciferin protein from seeds of Moringa oleifera

AU - Akrem, Ahmed

AU - Yousef, Nasser

AU - Begum, Afshan

AU - Negm, Amr

AU - Meyer, Arne

AU - Perbandt, Markus

AU - Buck, Friedrich

AU - Betzel, Christian

PY - 2014/6/1

Y1 - 2014/6/1

N2 - 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.

AB - 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.

U2 - 10.1007/s10930-014-9558-x

DO - 10.1007/s10930-014-9558-x

M3 - SCORING: Journal article

C2 - 24705831

VL - 33

SP - 253

EP - 257

JO - PROTEIN J

JF - PROTEIN J

SN - 1572-3887

IS - 3

ER -