Crystallographic characterization of tetanus toxin fragment C.
The C-terminal fragment from tetanus toxin has been crystallized. The 50 kDa protein forms prismatic crystals with an orthorhombic unit cell of dimensions a = 64.03 A, b = 76.31 A and c = 135.3 A. The space group is P2(1)2(1)2(1). Assuming one molecule per asymmetric unit, the solvent occupies 63% of the unit cell.
Anderson
M D
MD
Department of Chemistry, University of Glasgow, U.K.
Fairweather
N
N
Charles
I G
IG
Emsley
P
P
Isaacs
N W
NW
MacDermott
G
G
D003460:Crystallization; D007202:Indicators and Reagents; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D010843:Pichia / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D013744:Tetanus Toxin / Q000737:chemistry* / Q000302:isolation & purification; D014118:Toxins, Biological / Q000737:chemistry; D014961:X-Ray Diffraction
D007202:Indicators and Reagents; D010446:Peptide Fragments; D011994:Recombinant Proteins; D013744:Tetanus Toxin; D014118:Toxins, Biological; C040635:tetanus toxin fragment C