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Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab.
Acta Crystallogr D Biol Crystallogr. 1999 Jan; 55(Pt 1):276-8.AC

Abstract

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 A. Crystals diffracted to a resolution limit of 3.36 A 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 A3 Da-1 could be estimated.

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Authors+Show Affiliations

Malpeli G
Institute of Biochemical Sciences, Science Faculty, University of Parma, I-43100 Parma, Italy.
Zanotti G
No affiliation info available
Gliubich F
No affiliation info available
Rizzotto A
No affiliation info available
Nishida SK
No affiliation info available
Folli C
No affiliation info available
Berni R
No affiliation info available

MeSH

AnimalsAntibodies, MonoclonalAntigen-Antibody ComplexCrystallizationHumansImmunoglobulin Fab FragmentsMacromolecular SubstancesMicePrealbuminRetinol-Binding ProteinsX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10089423

Citation

Malpeli, G, et al. "Crystallization and Preliminary X-ray Data for the Human Transthyretin-retinol-binding Protein (RBP) Complex Bound to an anti-RBP Fab." Acta Crystallographica. Section D, Biological Crystallography, vol. 55, no. Pt 1, 1999, pp. 276-8.
Malpeli G, Zanotti G, Gliubich F, et al. Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):276-8.
Malpeli, G., Zanotti, G., Gliubich, F., Rizzotto, A., Nishida, S. K., Folli, C., & Berni, R. (1999). Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab. Acta Crystallographica. Section D, Biological Crystallography, 55(Pt 1), 276-8.
Malpeli G, et al. Crystallization and Preliminary X-ray Data for the Human Transthyretin-retinol-binding Protein (RBP) Complex Bound to an anti-RBP Fab. Acta Crystallogr D Biol Crystallogr. 1999;55(Pt 1):276-8. PubMed PMID: 10089423.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab. AU - Malpeli,G, AU - Zanotti,G, AU - Gliubich,F, AU - Rizzotto,A, AU - Nishida,S K, AU - Folli,C, AU - Berni,R, Y1 - 1999/01/01/ PY - 1998/01/22/received PY - 1998/05/29/accepted PY - 1999/3/25/pubmed PY - 2000/6/23/medline PY - 1999/3/25/entrez SP - 276 EP - 8 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 55 IS - Pt 1 N2 - 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 A. Crystals diffracted to a resolution limit of 3.36 A 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 A3 Da-1 could be estimated. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/10089423/Crystallization_and_preliminary_X_ray_data_for_the_human_transthyretin_retinol_binding_protein__RBP__complex_bound_to_an_anti_RBP_Fab_ L2 - http://scripts.iucr.org/cgi-bin/paper?S0907444998007860 DB - PRIME DP - Unbound Medicine ER -

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