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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Acta Crystallographica. Section D: Biological Crystallography
Vol/bind	56
Udgave nummer	Pt 5
Sider (fra-til)	637-9
Antal sider	3
ISSN	0907-4449
Status	Udgivet - maj 2000

Citationsformater

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.

I: Acta Crystallographica. Section D: Biological Crystallography, Bind 56, Nr. Pt 5, 05.2000, s. 637-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › 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.",

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",

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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

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