Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin
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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.
|Journal||Acta Crystallographica. Section D: Biological Crystallography|
|Issue number||Pt 5|
|Number of pages||3|
|Publication status||Published - May 2000|
- Blood Proteins, Computer Graphics, Crystallization, Crystallography, X-Ray, Formates, Humans, Lectins, Lectins, C-Type, Models, Molecular, Peptide Fragments, Protein Conformation, Recombinant Proteins, Solutions