Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus

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Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus. / Coronado, Mônika A; Georgieva, Dessislava; Buck, Friedrich; Gabdoulkhakov, Azat H; Ullah, Anwar; Spencer, Patrick J; Arni, Raghuvir K; Betzel, Christian.

in: ACTA CRYSTALLOGR F, Jahrgang 68, Nr. Pt 9, 01.09.2012, S. 1052-4.

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@article{3349e89e2f84411eb4118dac30b9584b,
title = "Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus",
abstract = "Crotamine, a highly basic myotoxic polypeptide (molecular mass 4881 Da) isolated from the venom of the Brazilian rattlesnake Crotalus durissus terrificus, causes skeletal muscle contraction and spasms, affects the functioning of voltage-sensitive sodium channels by inducing sodium influx and possesses antitumour activity, suggesting potential pharmaceutical applications. Crotamine was purified from C. durissus terrificus venom; the crystals diffracted to 1.9 {\AA} resolution and belonged to the orthorhombic space group I2(1)2(1)2(1) or I222, with unit-cell parameters a = 67.75, b = 74.4, c = 81.01 {\AA}. The self-rotation function indicated that the asymmetric unit contained three molecules. However, structure determination by molecular replacement using NMR-determined coordinates was unsuccessful and a search for potential derivatives has been initiated.",
keywords = "Animals, Crotalid Venoms, Crotalus, Crystallization, Crystallography, X-Ray",
author = "Coronado, {M{\^o}nika A} and Dessislava Georgieva and Friedrich Buck and Gabdoulkhakov, {Azat H} and Anwar Ullah and Spencer, {Patrick J} and Arni, {Raghuvir K} and Christian Betzel",
year = "2012",
month = sep,
day = "1",
doi = "10.1107/S1744309112032721",
language = "English",
volume = "68",
pages = "1052--4",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "Pt 9",

}

RIS

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of crotamine, a myotoxic polypeptide from the Brazilian snake Crotalus durissus terrificus

AU - Coronado, Mônika A

AU - Georgieva, Dessislava

AU - Buck, Friedrich

AU - Gabdoulkhakov, Azat H

AU - Ullah, Anwar

AU - Spencer, Patrick J

AU - Arni, Raghuvir K

AU - Betzel, Christian

PY - 2012/9/1

Y1 - 2012/9/1

N2 - Crotamine, a highly basic myotoxic polypeptide (molecular mass 4881 Da) isolated from the venom of the Brazilian rattlesnake Crotalus durissus terrificus, causes skeletal muscle contraction and spasms, affects the functioning of voltage-sensitive sodium channels by inducing sodium influx and possesses antitumour activity, suggesting potential pharmaceutical applications. Crotamine was purified from C. durissus terrificus venom; the crystals diffracted to 1.9 Å resolution and belonged to the orthorhombic space group I2(1)2(1)2(1) or I222, with unit-cell parameters a = 67.75, b = 74.4, c = 81.01 Å. The self-rotation function indicated that the asymmetric unit contained three molecules. However, structure determination by molecular replacement using NMR-determined coordinates was unsuccessful and a search for potential derivatives has been initiated.

AB - Crotamine, a highly basic myotoxic polypeptide (molecular mass 4881 Da) isolated from the venom of the Brazilian rattlesnake Crotalus durissus terrificus, causes skeletal muscle contraction and spasms, affects the functioning of voltage-sensitive sodium channels by inducing sodium influx and possesses antitumour activity, suggesting potential pharmaceutical applications. Crotamine was purified from C. durissus terrificus venom; the crystals diffracted to 1.9 Å resolution and belonged to the orthorhombic space group I2(1)2(1)2(1) or I222, with unit-cell parameters a = 67.75, b = 74.4, c = 81.01 Å. The self-rotation function indicated that the asymmetric unit contained three molecules. However, structure determination by molecular replacement using NMR-determined coordinates was unsuccessful and a search for potential derivatives has been initiated.

KW - Animals

KW - Crotalid Venoms

KW - Crotalus

KW - Crystallization

KW - Crystallography, X-Ray

U2 - 10.1107/S1744309112032721

DO - 10.1107/S1744309112032721

M3 - SCORING: Journal article

C2 - 22949192

VL - 68

SP - 1052

EP - 1054

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - Pt 9

ER -