Crystallization and preliminary X-ray studies of the VL domain of the antibody McPC603 produced in Escherichia coli.
The VL domain, obtained from a recombinant Fv fragment of the antibody McPC603 expressed in Escherichia coli, has been crystallized as a dimer from 2 M-(NH4)2SO4 (pH 4.0). The crystals are hexagonal, space group P6(1)22. The cell dimensions are a = b = 86.48 A, c = 76.64 A, with a VL monomer as the asymmetric unit. The crystals diffract to 2.0 A. The structure was solved by Patterson search using the VL domain of the Fab fragment of McPC603 and the VL dimer REI.
Glockshuber
R
R
Genzentrum, Universität, Martinsried, F.R.G.
Steipe
B
B
Huber
R
R
Plückthun
A
A
D002846:Chromatography, Affinity; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000276:immunology; D007070:Immunoglobulin A / Q000235:genetics; D007147:Immunoglobulin Light Chains / Q000235:genetics; D007135:Immunoglobulin Variable Region / Q000235:genetics; D010767:Phosphorylcholine; D011487:Protein Conformation; D011994:Recombinant Proteins; D013237:Stereoisomerism; D014961:X-Ray Diffraction
D007070:Immunoglobulin A; D007147:Immunoglobulin Light Chains; D007135:Immunoglobulin Variable Region; D011994:Recombinant Proteins; D010767:Phosphorylcholine