Helix packing and subunit conformation in horse spleen apoferritin

An electron density map of horse spleen apoferritin at 0.28-nm (2.8 Å) resolution and its preliminary interpretation have been described previously 1 . Rigorous examination of this and newer maps at the same nominal resolution but calculated from more extensive data sets, including model building in...

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Veröffentlicht in:	Nature (London) 1980-11, Vol.288 (5788), p.298-300
Hauptverfasser:	Clegg, George A., Stansfield, Robert F. D., Bourne, Philip E., Harrison, Pauline M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoproteins Ferritins Horses Humanities and Social Sciences Hydrogen Bonding letter Macromolecular Substances multidisciplinary Protein Conformation Science Science (multidisciplinary) Spleen X-Ray Diffraction
Online-Zugang:	Volltext
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