Abstract
Crystals of the small Hydrophobic protein crambin have been shown to diffract to a resolution of at least 0.88 Å (11). This means that crambin presents a rare opportunity to study a protein structure at virtually atomic resolution. The high resolution of the diffraction pattern coupled with the assets of neutron diffraction present the distinct possibility that crambin’s analysis may surpass that of any other protein system in degree and accuracy of detail.
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Teeter, M.M., Kossiakoff, A.A. (1984). The Neutron Structure of the Hydrophobic Plant Protein Crambin. In: Schoenborn, B.P. (eds) Neutrons in Biology. Basic Life Sciences, vol 27. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0375-4_20
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DOI: https://doi.org/10.1007/978-1-4899-0375-4_20
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