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

0575416 - BTÚ 2024 RIV GB eng J - Journal Article
Kolenko, Petr - Mikulecký, Pavel - Pham, Phuong Ngoc - Malý, Martin - Schneider, Bohdan
Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10.
Journal of Applied Crystallography. Roč. 56, part 4 (2023), s. 1261-1266. ISSN 0021-8898. E-ISSN 1600-5767
R&D Projects: GA MŠMT EF16_019/0000778; GA MŠMT(CZ) LM2018127
Institutional support: RVO:86652036
Keywords : anisotropy * paired refinement * binder H33
OECD category: Analytical chemistry
Impact factor: 6.1, year: 2022
Method of publishing: Open access
https://scripts.iucr.org/cgi-bin/paper?S160057672300479X

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 angstrom. The structure of binder H33 belongs to the 2% of crystal structures with the highest solvent content in the Protein Data Bank.
Permanent Link: https://hdl.handle.net/11104/0345865