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Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
Petr Kolenko1,2, Pavel Mikulecký2, Phuong Ngoc Pham2
1Czech Technical University in Prague, Brehova 7, Prague 115 19, Czech Republic.
Abstract:
Binder H33 is a small protein binder engineered by ribosome display to bind human interleukin 10. Crystals of binder H33 display severe diffraction anisotropy. A set of data files with correction for diffraction anisotropy based on different local signal-to-noise ratios was prepared. Paired refinement was used to find the optimal anisotropic high-resolution diffraction limit of the data: 3.13-2.47 Å. The structure of binder H33 belongs to the 2% of crystal structures with the highest solvent content in the Protein Data Bank.
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