Structure of horse-spleen apoferritin at 6 Å resolution

Details Structure of horse-spleen apoferritin at 6 Å resolution Structure of horse-spleen apoferritin at 6 Å resolution

Jun 1975

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1975natur.255..653h&link_type=abstract

Nature, Volume 255, Issue 5510, pp. 653-654 (1975).

Physics

2

Scientific paper

FERRITIN is the principal iron storage molecule in a wide variety of organisms1. It consists of a hollow protein shell (apoferritin) which can contain up to its own weight of hydrous ferric oxide-phosphate as a microcrystalline micelle. Both the shell and its contents have been observed in electron micrographs2,3. Ferritin and apoferritin crystallise in a number of forms, including a cubic one in which the round molecules are ``close-packed''4. The cubic crystals have space group F432 (No. 209), side a = 184Å, and contain four molecules per unit cell4. We report here on the electron density map of cubic horse-spleen apoferritin at 6-Å resolution which we have obtained using two isomorphous derivatives, formed with parachloro-mercury benzoic acid (PCMB) and uranyl nitrate.

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