Comparative structural analysis of a histone-like protein from Spiroplasma melliferum in the crystalline state and in solution |
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| Institution: | 1. National Research Center ‘Kurchatov Institute’, 123182 Moscow, Russian Federation;2. A. V. Shubnikov Institute of Crystallography, FSRC ‘Crystallography and Photonics’, Russian Academy of Sciences, 119333 Moscow, Russian Federation;3. M. M. Shemyakin–Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russian Federation |
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| 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. |
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| 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 |
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