Ladislau C Kovari, Cory Momany, Michael G Rossmann Structure

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The use of antibody fragments for crystallization and structure determinations Ladislau C Kovari, Cory Momany, Michael G Rossmann Structure Volume 3, Issue 12, Pages 1291-1293 (December 1995) DOI: 10.1016/S0969-2126(01)00266-0

Figure 1 . Fab purification using a linear programmed pH gradient, from 8.0 to 5.8, for elution from a Pharmacia MonoQ column. Nine different fractions of the Fab could be recognized, but only fraction VII crystallized easily when complexed with HIV p24. Structure 1995 3, 1291-1293DOI: (10.1016/S0969-2126(01)00266-0)

Figure 2 . Native PAGE gel (8% to 25% cross-linked) analysis of molar ratios of HIV p24 and Fab. The p24 and Fab superimpose on the same band, but the p24–Fab complex exhibits retarded migration. A molar ratio of two p24s to one Fab appears to be the correct stoichiometry, although they occur as a 1:1 ratio in the crystal structure. Structure 1995 3, 1291-1293DOI: (10.1016/S0969-2126(01)00266-0)