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• W2079846965 abstract "The recombinant N-terminal domain of human ephrin type-A receptor 2 (rEphA2) has been crystallized in complex with the recombinantly produced Fab fragment of a fully human antibody (1C1; IgG1/κ). These are the first reported crystals of an ephrin receptor bound to an antibody. The orthorhombic crystals belonged to space group C2221 (the 00l reflections obey the l = 2n rule), with unit-cell parameters a = 78.93, b = 120.79, c = 286.20 Å. The diffraction of the crystals extended to 2.0 Å resolution. However, only data to 2.55 Å resolution were considered to be useful owing to spot overlap caused by the long unit-cell parameter. The asymmetric unit is most likely to contain two 1C1 Fab–rEphA2 complexes. This corresponds to a crystal volume per protein weight (VM) of 2.4 Å3 Da−1 and a solvent content of 49.5%. The three-dimensional structure of this complex will shed light on the molecular basis of 1C1 specificity. This will also contribute to a better understanding of the mechanism of action of this antibody, the current evaluation of which as an antibody–drug conjugate in cancer therapy makes it a particularly interesting case study." @default.
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• W2079846965 date "2010-05-29" @default.
• W2079846965 modified "2023-09-26" @default.
• W2079846965 title "Crystallization and preliminary X-ray diffraction analysis of the complex of a human anti-ephrin type-A receptor 2 antibody fragment and its cognate antigen" @default.
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• W2079846965 doi "https://doi.org/10.1107/s1744309110015861" @default.
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