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:
Short Communications
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
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author Kolenko, Petr
Mikulecký, Pavel
Pham, Phuong Ngoc
Malý, Martin
Schneider, Bohdan
author_facet Kolenko, Petr
Mikulecký, Pavel
Pham, Phuong Ngoc
Malý, Martin
Schneider, Bohdan
author_sort Kolenko, Petr
collection PubMed
description 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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spelling pubmed-104055932023-08-08 Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10 Kolenko, Petr Mikulecký, Pavel Pham, Phuong Ngoc Malý, Martin Schneider, Bohdan J Appl Crystallogr Short Communications 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. International Union of Crystallography 2023-06-16 /pmc/articles/PMC10405593/ /pubmed/37555209 http://dx.doi.org/10.1107/S160057672300479X Text en © Petr Kolenko et al. 2023 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Short Communications
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
title Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
title_full Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
title_fullStr Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
title_full_unstemmed Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
title_short Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10
title_sort diffraction anisotropy and paired refinement: crystal structure of h33, a protein binder to interleukin 10
topic Short Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10405593/
https://www.ncbi.nlm.nih.gov/pubmed/37555209
http://dx.doi.org/10.1107/S160057672300479X
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