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Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10

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 refineme...

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Detalles Bibliográficos
Autores principales: Kolenko, Petr, Mikulecký, Pavel, Pham, Phuong Ngoc, Malý, Martin, Schneider, Bohdan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10405593/
https://www.ncbi.nlm.nih.gov/pubmed/37555209
http://dx.doi.org/10.1107/S160057672300479X
Descripción
Sumario: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.