Crystallization and preliminary X-ray diffraction analysis of the complex between a human anti-interferon antibody fragment and human interferon α-2A

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Abstract

Recombinant human interferon α-2A (rhIFN-α-2A) has been crystallized in complex with the recombinantly produced Fab fragment of a therapeutic monoclonal antibody (MEDI545; IgG1/κ) which targets several human interferon α subtypes. This constitutes the first reported crystals of a human type I interferon bound to an antibody. The orthorhombic crystals belonged to either space group I222 or I212121, with unit-cell parameters a = 134.82, b = 153.26, c = 163.49 Å. The diffraction of the crystals extended to 3.0 Å resolution. The asymmetric unit contained two Fab-rhIFN-α-2A complexes. This corresponded to a crystal volume per protein weight (VM) of 3.02 Å3 Da-1 and a solvent content of 59.3%. The corresponding three-dimensional structure is expected to shed light on the mechanism of action of MEDI545 and the molecular basis of its specificity. © Oganesyan et al. 2009.

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APA

Oganesyan, V., Damschroder, M. M., Cook, K. E., Wu, H., & Dall’Acqua, W. F. (2009). Crystallization and preliminary X-ray diffraction analysis of the complex between a human anti-interferon antibody fragment and human interferon α-2A. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(1), 14–16. https://doi.org/10.1107/S1744309108037925

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