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Selected Publication:

Brooks, CL; Blackler, RJ; Gerstenbruch, S; Kosma, P; Müller-Loennies, S; Brade, H; Evans, SV.
(2008): Pseudo-symmetry and twinning in crystals of homologous antibody Fv fragments.
Acta Crystallogr D Biol Crystallogr. 2008; 64(Pt 12):1250-1258 FullText FullText_BOKU

A difference of seven conservative amino-acid substitutions between two single-chain antibodies (scFvs) specific for chlamydial lipopolysaccharide does not significantly affect their molecular structures or packing contacts, but dramatically affects their crystallization. The structure of the variable domain (Fv) of SAG173-04 was solved to 1.86 angstrom resolution and an R-cryst of 18.9% in space group P2(1)2(1)2(1). Crystals of the homologous SAG506-01 diffracted to 1.95 angstrom resolution and appeared at first to have Patterson symmetry I4/m or P4/mmm; however, no solution could be found in space groups belonging to the former and refinement in the only solution corresponding to the latter (in space group P4(3)2(1)2) stalled at R-free = 30.0%. Detailed examination of the diffraction data revealed that the crystal was likely to be twinned and that the correct space group was P2(1)2(1)2(1). Both translational pseudo-symmetry and pseudo-merohedral twinning were observed in one crystal of SAG506-01 and pseudo-merohedral twinning was observed for a second crystal. The final R factor for SAG506-01 after refinement in P2(1)2(1)2(1) was 20.5%.
Authors BOKU Wien:
Kosma Paul
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Antibodies, Monoclonal - chemistry
Chlamydiaceae -
Cloning, Molecular -
Complementarity Determining Regions - chemistry
Crystallization -
Epitopes -
Lipopolysaccharides - chemistry
Molecular Sequence Data -
Mutation -
Peptide Library -
Protein Structure, Tertiary -
Species Specificity -
Structural Homology, Protein -
Structure-Activity Relationship -

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