Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectin.
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.
Nielsen
B B
BB
Department of Medicinal Chemistry, Royal Danish School of Pharmacy, DK-2100 Copenhagen, Denmark. bettina@medchem.dfh.dk
Kastrup
J S
JS
Rasmussen
H
H
Graversen
J H
JH
Etzerodt
M
M
Thøgersen
H C
HC
Larsen
I K
IK
D001798:Blood Proteins / Q000737:chemistry*; D003196:Computer Graphics; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D005561:Formates; D006801:Humans; D037102:Lectins / Q000737:chemistry; D037181:Lectins, C-Type; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012996:Solutions
D001798:Blood Proteins; D005561:Formates; D037102:Lectins; D037181:Lectins, C-Type; D010446:Peptide Fragments; D011994:Recombinant Proteins; D012996:Solutions; C030544:formic acid; C048648:tetranectin