Abstract
X-ray small angle scattering patterns of solutions and gels of native chicken erythrocyte chromatin and chromatin depleted of H5 histones have been measured under several ionic conditions using synchrotron radiation. Features of the patterns are interpreted as resulting from a superstructure with an outer diameter of about 300A which is already present in uncondensed nucleofilaments. This superstructure which is shown to be maintained by the H5 histones also explains the rapid condensation of the nucleofilaments in higher ionic strengths.
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