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

Betina Bryde Nielsen; Jette Sandholm Jensen Kastrup; Hanne B. Rasmussen; J H Graversen; Michael Etzerodt; Hans Christian Thøgersen; Ingrid K. Larsen

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

Betina Bryde Nielsen, Jette Sandholm Jensen Kastrup, Hanne B. Rasmussen, J H Graversen, Michael Etzerodt, Hans Christian Thøgersen, Ingrid K. Larsen

4 Citations (Scopus)

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.

Original language	English
Journal	Acta Crystallographica. Section D: Biological Crystallography
Volume	56
Issue number	Pt 5
Pages (from-to)	637-9
Number of pages	3
ISSN	0907-4449
Publication status	Published - May 2000

Keywords

Blood Proteins
Computer Graphics
Crystallization
Crystallography, X-Ray
Formates
Humans
Lectins
Lectins, C-Type
Models, Molecular
Peptide Fragments
Protein Conformation
Recombinant Proteins
Solutions

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Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin. / Nielsen, Betina Bryde; Kastrup, Jette Sandholm Jensen; Rasmussen, Hanne B. et al.

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

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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.",

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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",

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publisher = "International Union of Crystallography",

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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

SN - 2059-7983

VL - 56

SP - 637

EP - 639

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

IS - Pt 5

ER -

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

Abstract

Keywords

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