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Crystallization of human complement component C5

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Standard

Crystallization of human complement component C5. / Discipio, R G; Jenner, L; Thirup, S; Sottrup-Jensen, L; Nyborg, J; Stura, E.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 54, No. Pt 4, 1998, p. 643-6.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Discipio, RG, Jenner, L, Thirup, S, Sottrup-Jensen, L, Nyborg, J & Stura, E 1998, 'Crystallization of human complement component C5', Acta Crystallographica. Section D: Biological Crystallography, vol. 54, no. Pt 4, pp. 643-6.

APA

Discipio, R. G., Jenner, L., Thirup, S., Sottrup-Jensen, L., Nyborg, J., & Stura, E. (1998). Crystallization of human complement component C5. Acta Crystallographica. Section D: Biological Crystallography, 54(Pt 4), 643-6.

CBE

Discipio RG, Jenner L, Thirup S, Sottrup-Jensen L, Nyborg J, Stura E. 1998. Crystallization of human complement component C5. Acta Crystallographica. Section D: Biological Crystallography. 54(Pt 4):643-6.

MLA

Discipio, R G et al. "Crystallization of human complement component C5". Acta Crystallographica. Section D: Biological Crystallography. 1998, 54(Pt 4). 643-6.

Vancouver

Discipio RG, Jenner L, Thirup S, Sottrup-Jensen L, Nyborg J, Stura E. Crystallization of human complement component C5. Acta Crystallographica. Section D: Biological Crystallography. 1998;54(Pt 4):643-6.

Author

Discipio, R G ; Jenner, L ; Thirup, S ; Sottrup-Jensen, L ; Nyborg, J ; Stura, E. / Crystallization of human complement component C5. In: Acta Crystallographica. Section D: Biological Crystallography. 1998 ; Vol. 54, No. Pt 4. pp. 643-6.

Bibtex

@article{cb0f7300f9bf11dd8f9a000ea68e967b,
title = "Crystallization of human complement component C5",
abstract = "Human complement component C5 has been crystallized using a low-salt batch technique. The crystals are large hexagonal bi-pyramids often larger than 1.5 mm. Although these crystals were grown in low salt (0.1 M NaCl), they are remarkably stable for at least 2 months at 281 K and they are not dissolved in aqueous buffers containing up to 2 M sodium chloride. The space group is P3121 or P3221, and the cell parameters were determined to be a = 144.9, b = 144.9, c = 243.1 A; alpha = 90 degrees, beta = 90, gamma = 120 degrees. At room temperature and cryo-temperatures the crystals diffract at best to 6 A using rotating-anode X-ray sources. Using synchrotron radiation with cryoprotection using 40%(v/v) PEG 400 the resolution limit can be extended to 3.3 A. In both cases the crystals show significant anisotropy, with relatively weaker reflections at higher resolution in the a*b* plane.",
keywords = "Anisotropy, Complement C5, Crystallization, Crystallography, X-Ray, Humans, Protein Conformation, Synchrotrons",
author = "Discipio, {R G} and L Jenner and S Thirup and L Sottrup-Jensen and J Nyborg and E Stura",
year = "1998",
language = "English",
volume = "54",
pages = "643--6",
journal = "Acta crystallographica Section D: Structural biology ",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 4",

}

RIS

TY - JOUR

T1 - Crystallization of human complement component C5

AU - Discipio, R G

AU - Jenner, L

AU - Thirup, S

AU - Sottrup-Jensen, L

AU - Nyborg, J

AU - Stura, E

PY - 1998

Y1 - 1998

N2 - Human complement component C5 has been crystallized using a low-salt batch technique. The crystals are large hexagonal bi-pyramids often larger than 1.5 mm. Although these crystals were grown in low salt (0.1 M NaCl), they are remarkably stable for at least 2 months at 281 K and they are not dissolved in aqueous buffers containing up to 2 M sodium chloride. The space group is P3121 or P3221, and the cell parameters were determined to be a = 144.9, b = 144.9, c = 243.1 A; alpha = 90 degrees, beta = 90, gamma = 120 degrees. At room temperature and cryo-temperatures the crystals diffract at best to 6 A using rotating-anode X-ray sources. Using synchrotron radiation with cryoprotection using 40%(v/v) PEG 400 the resolution limit can be extended to 3.3 A. In both cases the crystals show significant anisotropy, with relatively weaker reflections at higher resolution in the a*b* plane.

AB - Human complement component C5 has been crystallized using a low-salt batch technique. The crystals are large hexagonal bi-pyramids often larger than 1.5 mm. Although these crystals were grown in low salt (0.1 M NaCl), they are remarkably stable for at least 2 months at 281 K and they are not dissolved in aqueous buffers containing up to 2 M sodium chloride. The space group is P3121 or P3221, and the cell parameters were determined to be a = 144.9, b = 144.9, c = 243.1 A; alpha = 90 degrees, beta = 90, gamma = 120 degrees. At room temperature and cryo-temperatures the crystals diffract at best to 6 A using rotating-anode X-ray sources. Using synchrotron radiation with cryoprotection using 40%(v/v) PEG 400 the resolution limit can be extended to 3.3 A. In both cases the crystals show significant anisotropy, with relatively weaker reflections at higher resolution in the a*b* plane.

KW - Anisotropy

KW - Complement C5

KW - Crystallization

KW - Crystallography, X-Ray

KW - Humans

KW - Protein Conformation

KW - Synchrotrons

M3 - Journal article

C2 - 9761862

VL - 54

SP - 643

EP - 646

JO - Acta crystallographica Section D: Structural biology

JF - Acta crystallographica Section D: Structural biology

SN - 2059-7983

IS - Pt 4

ER -