Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab

• Published in: Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-01, Vol.55 (1), p.276-278
• Main Authors: Malpeli, Giorgio, Zanotti, Giuseppe, Gliubich, Francesca, Rizzotto, Andrea, Nishida, Sonia K., Folli, Claudia, Berni, Rodolfo
• Format: Article
• Language: English
• Subjects: Animals; Antibodies, Monoclonal - chemistry; Antibodies, Monoclonal - isolation & purification; Antigen-Antibody Complex - chemistry; Antigen-Antibody Complex - isolation & purification; Crystallization; Humans; Immunoglobulin Fab Fragments - chemistry; Immunoglobulin Fab Fragments - isolation & purification; Macromolecular Substances; Mice; Prealbumin - chemistry; Prealbumin - immunology; Prealbumin - isolation & purification; Retinol-Binding Proteins - chemistry; Retinol-Binding Proteins - immunology; Retinol-Binding Proteins - isolation & purification; transthyretin (human); X-Ray Diffraction
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444998007860

A macromolecular complex of human transthyretin, human retinol‐binding protein and an anti‐retinol‐binding‐protein Fab was crystallized by vapour diffusion in sitting drops. Diffraction from these crystals at cryogenic temperatures was consistent with the space group C222, with cell parameters a = 159.34, b = 222.40 and c = 121.27 Å. Crystals diffracted to a resolution limit of 3.36 Å using synchrotron radiation. Based on a 2:2:1 stoichiometry for the Fab–retinol‐binding‐protein–transthyretin complex and the presence of one such complex per asymmetric unit, a reasonable Vm coefficient of 2.74 Å3 Da−1 could be estimated.