Yu. A. Gaponov, V. I. Timofeev, Yu. K. Agapova, E. V. Bocharov, E. V. Shtykova, T. V. Rakitina, “Comparative structural analysis of a histone-like protein from <i>Spiroplasma melliferum</i> in the crystalline state and in solution”, Mendeleev Commun., 2022, Volume 32, Issue 6,Pages <nobr>742

This article is cited in 4 papers

Communications

Comparative structural analysis of a histone-like protein from Spiroplasma melliferum in the crystalline state and in solution

Yu. A. Gaponov^a, V. I. Timofeev^ab, Yu. K. Agapova^a, E. V. Bocharov^c, E. V. Shtykova^b, T. V. Rakitina^ac

^a National Research Centre 'Kurchatov Institute', Moscow, Russian Federation
^b A.V. Shubnikov Institute of Crystallography, FSRC ‘Crystallography and Photonics', Russian Academy of Sciences, Moscow, Russian Federaion
^c M.M. Shemyakin–Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation

Abstract: A solution of a histone-like protein from Spiroplasma melliferum (HUSpm) was examined by small-angle X-ray scattering (SAXS). The experimental SAXS curve was compared with those calculated for the HUSpm structures from the PDB databank obtained by both X-ray diffraction analysis and nuclear magnetic resonance spectroscopy. The model of the HUSpm structure in solution, which best agrees with the experimental SAXS data, has a shorter distance between the centers of mass of the HUSpm monomers compared to the crystal structure, indicating that the HUSpm monomers can be located closer to each other in solution than in the crystalline state.

Keywords: small-angle X-ray scattering, SAXS, X-ray diffraction, XRD, nuclear magnetic resonance spectroscopy, NMR, crystal structure, structure in solution, histone-like HU protein.

Language: English

DOI: 10.1016/j.mencom.2022.11.011