The polymerization of actin: structural changes from small-angle neutron scattering.

Alexander I. Norman, Robert Ivkov, Jeffrey G. Forbes, Sandra C. Greer

Research output: Contribution to journalArticlepeer-review


We present a new analysis of small-angle neutron-scattering data from rabbit muscle actin in the course of the polymerization from G-actin to F-actin as a function of temperature. The data, from Ivkov et al. [J. Chem. Phys. 108, 5599 (1998)], were taken in D2O buffer with Ca2+ as the divalent cation on the G-actin in the presence of ATP and with KCl as the initiating salt. The new analysis of the data using modeling and the method of generalized indirect fourier transform (O. Glatter, GIFT, University of Graz, Austria, provide shapes and dimensions of the G-actin monomer and of the growing actin oligomer in solution as a function of temperature and salt concentration. This analysis indicates that the G-actin monomer, under the conditions given above, is a sphere 50-54 A in diameter as opposed to the oblate ellipsoid seen by x-ray crystallography. The F-actin dimensions are consistent with x-ray crystal structure determinations.

Original languageEnglish (US)
Pages (from-to)154904
Number of pages1
JournalThe Journal of Chemical Physics
Issue number15
StatePublished - Oct 15 2005
Externally publishedYes

ASJC Scopus subject areas

  • Atomic and Molecular Physics, and Optics


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