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Journal Article

Crystals of an antibody FV fragment against an integral membrane protein diffracting to 1.28 Å resolution

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Ostermeier,  Christian
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Essen,  Lars-Oliver
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Ostermeier, C., Essen, L.-O., & Michel, H. (1995). Crystals of an antibody FV fragment against an integral membrane protein diffracting to 1.28 Å resolution. Proteins: Structure, Function, and Bioinformatics, 21, 74-77. doi:10.1002/prot.340210110.


Cite as: https://hdl.handle.net/21.11116/0000-0007-081B-3
Abstract
The Fv fragment of a monoclonal antibody, 7E2 (IgG1, κ, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans, was cloned and produced in Escherichia coli. Crystals suitable for highresolution X‐ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P212121 with unit cell dimensions of a = 51.51 Å, b = 56.15 Å, c = 99.86 Å (1 Å = 0.1 nm) and contain one Fv fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 Å resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics