Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin. / Nielsen, Betina Bryde; Kastrup, Jette Sandholm Jensen; Rasmussen, Hanne B.; Graversen, J H; Etzerodt, Michael; Thøgersen, Hans Christian; Larsen, Ingrid K.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 56, No. Pt 5, 05.2000, p. 637-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nielsen, BB, Kastrup, JSJ, Rasmussen, HB, Graversen, JH, Etzerodt, M, Thøgersen, HC & Larsen, IK 2000, 'Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin', Acta Crystallographica. Section D: Biological Crystallography, vol. 56, no. Pt 5, pp. 637-9.

APA

Nielsen, B. B., Kastrup, J. S. J., Rasmussen, H. B., Graversen, J. H., Etzerodt, M., Thøgersen, H. C., & Larsen, I. K. (2000). Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin. Acta Crystallographica. Section D: Biological Crystallography, 56(Pt 5), 637-9.

Vancouver

Nielsen BB, Kastrup JSJ, Rasmussen HB, Graversen JH, Etzerodt M, Thøgersen HC et al. Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin. Acta Crystallographica. Section D: Biological Crystallography. 2000 May;56(Pt 5):637-9.

Author

Nielsen, Betina Bryde ; Kastrup, Jette Sandholm Jensen ; Rasmussen, Hanne B. ; Graversen, J H ; Etzerodt, Michael ; Thøgersen, Hans Christian ; Larsen, Ingrid K. / Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin. In: Acta Crystallographica. Section D: Biological Crystallography. 2000 ; Vol. 56, No. Pt 5. pp. 637-9.

Bibtex

@article{64b3a8ee68d747178246b0fccd4a38fa,
title = "Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin",
abstract = "The two C-terminal domains, TN23 (residues 17-181), of human recombinant tetranectin, a plasminogen kringle 4 binding C-type lectin, have been crystallized in two different space groups. Using PEG 8000 as precipitant and at a pH of 8.5, crystals belonging to the monoclinic space group C2 are obtained, with unit-cell parameters a = 160.4, b = 44.7, c = 107.5 A, beta = 127.6 degrees. Using sodium formate as precipitant and at a pH of 5.0, TN23 crystallizes in a rhombohedral space group, with unit-cell parameters a = b = c = 107.4 A, alpha = beta = gamma = 78.3 degrees. A full data set to 4.5 A has been collected from the monoclinic crystals. Using the structure of full-length tetranectin, a molecular-replacement solution has been obtained. The crystal packing shows that TN23 crystallizes as a trimer, with one trimer in the asymmetric unit.",
keywords = "Blood Proteins, Computer Graphics, Crystallization, Crystallography, X-Ray, Formates, Humans, Lectins, Lectins, C-Type, Models, Molecular, Peptide Fragments, Protein Conformation, Recombinant Proteins, Solutions",
author = "Nielsen, {Betina Bryde} and Kastrup, {Jette Sandholm Jensen} and Rasmussen, {Hanne B.} and Graversen, {J H} and Michael Etzerodt and Th{\o}gersen, {Hans Christian} and Larsen, {Ingrid K.}",
year = "2000",
month = may,
language = "English",
volume = "56",
pages = "637--9",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "Pt 5",

}

RIS

TY - JOUR

T1 - Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin

AU - Nielsen, Betina Bryde

AU - Kastrup, Jette Sandholm Jensen

AU - Rasmussen, Hanne B.

AU - Graversen, J H

AU - Etzerodt, Michael

AU - Thøgersen, Hans Christian

AU - Larsen, Ingrid K.

PY - 2000/5

Y1 - 2000/5

N2 - The two C-terminal domains, TN23 (residues 17-181), of human recombinant tetranectin, a plasminogen kringle 4 binding C-type lectin, have been crystallized in two different space groups. Using PEG 8000 as precipitant and at a pH of 8.5, crystals belonging to the monoclinic space group C2 are obtained, with unit-cell parameters a = 160.4, b = 44.7, c = 107.5 A, beta = 127.6 degrees. Using sodium formate as precipitant and at a pH of 5.0, TN23 crystallizes in a rhombohedral space group, with unit-cell parameters a = b = c = 107.4 A, alpha = beta = gamma = 78.3 degrees. A full data set to 4.5 A has been collected from the monoclinic crystals. Using the structure of full-length tetranectin, a molecular-replacement solution has been obtained. The crystal packing shows that TN23 crystallizes as a trimer, with one trimer in the asymmetric unit.

AB - The two C-terminal domains, TN23 (residues 17-181), of human recombinant tetranectin, a plasminogen kringle 4 binding C-type lectin, have been crystallized in two different space groups. Using PEG 8000 as precipitant and at a pH of 8.5, crystals belonging to the monoclinic space group C2 are obtained, with unit-cell parameters a = 160.4, b = 44.7, c = 107.5 A, beta = 127.6 degrees. Using sodium formate as precipitant and at a pH of 5.0, TN23 crystallizes in a rhombohedral space group, with unit-cell parameters a = b = c = 107.4 A, alpha = beta = gamma = 78.3 degrees. A full data set to 4.5 A has been collected from the monoclinic crystals. Using the structure of full-length tetranectin, a molecular-replacement solution has been obtained. The crystal packing shows that TN23 crystallizes as a trimer, with one trimer in the asymmetric unit.

KW - Blood Proteins

KW - Computer Graphics

KW - Crystallization

KW - Crystallography, X-Ray

KW - Formates

KW - Humans

KW - Lectins

KW - Lectins, C-Type

KW - Models, Molecular

KW - Peptide Fragments

KW - Protein Conformation

KW - Recombinant Proteins

KW - Solutions

M3 - Journal article

C2 - 10771434

VL - 56

SP - 637

EP - 639

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 5

ER -

ID: 44729417