Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain

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Standard

Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain. / Vognsen, Tina; Möller, Ingvar Rúnar; Kristensen, Ole.

I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, Bind 67, Nr. Pt 1, 01.01.2011, s. 48-50.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Vognsen, T, Möller, IR & Kristensen, O 2011, 'Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain', Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, bind 67, nr. Pt 1, s. 48-50. https://doi.org/10.1107/S1744309110042156

APA

Vognsen, T., Möller, I. R., & Kristensen, O. (2011). Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 67(Pt 1), 48-50. https://doi.org/10.1107/S1744309110042156

Vancouver

Vognsen T, Möller IR, Kristensen O. Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2011 jan. 1;67(Pt 1):48-50. https://doi.org/10.1107/S1744309110042156

Author

Vognsen, Tina ; Möller, Ingvar Rúnar ; Kristensen, Ole. / Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain. I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 2011 ; Bind 67, Nr. Pt 1. s. 48-50.

Bibtex

@article{a982121aa97144e7bdd850d6992800f1,
title = "Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain",
abstract = "The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 {\AA} resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 {\AA}. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Tina Vognsen and M{\"o}ller, {Ingvar R{\'u}nar} and Ole Kristensen",
year = "2011",
month = jan,
day = "1",
doi = "10.1107/S1744309110042156",
language = "English",
volume = "67",
pages = "48--50",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 1",

}

RIS

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction of the G3BP1 NTF2-like domain

AU - Vognsen, Tina

AU - Möller, Ingvar Rúnar

AU - Kristensen, Ole

PY - 2011/1/1

Y1 - 2011/1/1

N2 - The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.

AB - The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. Crystals were obtained using the hanging-drop vapour-diffusion method. Diffraction data were collected to 3.6 Å resolution using synchrotron radiation. The crystals belonged to the hexagonal space group P6(3)22, with unit-cell parameters a=b=89.84, c=70.02 Å. The crystals contained one molecule per asymmetric unit, with an estimated solvent content of 56%. Initial phases were obtained by molecular replacement.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1107/S1744309110042156

DO - 10.1107/S1744309110042156

M3 - Journal article

C2 - 21206022

VL - 67

SP - 48

EP - 50

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 1

ER -

ID: 33812118