Abstract
Abstract Electron paramagnetic resonance spectra of single crystals of myoglobin fluoride and hemoglobin fluoride were recorded at both cryogenic and ambient temperatures. Analysis of angular variations of line widths at these temperatures indicates that the misorientation of the heme plane in myoglobin crystals, which is considered responsible for the unusually broad resonance lines in these crystals, is not an artifact of the freezing process, but a characteristic inherent to the protein crystals as they are grown. Single crystal electron paramagnetic resonance spectroscopy at ambient temperature opens the possibility of the determination of the intracrystalline orientation of the heme groups in other hemoprotein crystals, the structure of which is readily damaged upon freezing.
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