Abstract
From the first days of protein neutron structure determination sperm whale myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol. Biol. 220 (1991) 381]. Nevertheless myoglobin is still of interest [Proc. Natl. Acad. Sci. USA 97 (2000) 3872]. The feasibility of the monochromatic neutron diffractometer BIX-3 at the JRR-3M reactor at the JAERI [J. Phys. Chem. Solids 60 (1999) 1623], to collect high-resolution diffraction data in a relatively short time stimulated us to repeat the structural determination of myoglobin. The structure of metmyoglobin has been determined up to a resolution of 1.5 Å. The hydrogen atoms were replaced in part, by deuterium soaking the crystals for more than 10 years in D2O. A refinement of all atoms has been performed including the refinement of individual mean square displacements and occupancies of the exchangeable protons in backbone hydrogen bonds. A method is described to show clear negative scattering densities of the H atoms. Water molecules within the protein and on the molecule surface are shown. The exchangeability of H atoms is correlated with structural distribution and flexibility.
Originalsprache | Englisch |
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Seiten (von - bis) | 183-193 |
Seitenumfang | 11 |
Fachzeitschrift | Biophysical Chemistry |
Jahrgang | 95 |
Ausgabenummer | 3 |
DOIs | |
Publikationsstatus | Veröffentlicht - 28 März 2002 |