title: Crystallographic characterization of tetanus toxin fragment C.
abstract: 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.
authors: Department of Chemistry, University of Glasgow, U.K.
authors: M D
authors: MD
authors: Anderson
authors: N
authors: N
authors: Fairweather
authors: I G
authors: IG
authors: Charles
authors: P
authors: P
authors: Emsley
authors: N W
authors: NW
authors: Isaacs
authors: G
authors: G
authors: MacDermott
mesh_terms: 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
chemical_list: D007202:Indicators and Reagents; D010446:Peptide Fragments; D011994:Recombinant Proteins; D013744:Tetanus Toxin; D014118:Toxins, Biological; C040635:tetanus toxin fragment C