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Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
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SYSNO ASEP 0575416 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10 Author(s) Kolenko, Petr (BTO-N) ORCID, RID
Mikulecký, Pavel (BTO-N) RID
Pham, Phuong Ngoc (BTO-N)
Malý, Martin (BTO-N) ORCID
Schneider, Bohdan (BTO-N) RID, ORCIDNumber of authors 5 Source Title Journal of Applied Crystallography. - : Wiley - ISSN 0021-8898
Roč. 56, part 4 (2023), s. 1261-1266Number of pages 6 s. Language eng - English Country GB - United Kingdom Keywords anisotropy ; paired refinement ; binder H33 Subject RIV CB - Analytical Chemistry, Separation OECD category Analytical chemistry R&D Projects EF16_019/0000778 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2018127 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support BTO-N - RVO:86652036 UT WOS 001046279800034 EID SCOPUS 85168131794 DOI 10.1107/S160057672300479X Annotation 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. Workplace Institute of Biotechnology Contact Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Year of Publishing 2024 Electronic address https://scripts.iucr.org/cgi-bin/paper?S160057672300479X
Number of the records: 1