Chemical cross‐linking with dithiobis(succinimidyl propionate) has been used to investigate the relative disposition of neighbouring H5 (H1) molecules in chicken erythrocyte chromatin in the extended (nucleosome filament) and condensed (300 A filament) states; in this chromatin H5 and H1 are interspersed along the nucleosome filament, rather than segregated into blocks, as shown by the nature of the cross‐linked dimers and their relative amounts. Detailed analysis of the cross‐linked H5 homopolymers from extended chromatin and condensed nuclear chromatin indicates which domains of H5 are in contact (or close proximity) in the two states. Two results suggest a polar, head‐to‐tail arrangement of H5 molecules along the nucleosome filament. This arrangement persists when chromatin adopts higher‐order structure but in the folded state neighbouring basic C‐terminal domains, in particular, are more closely juxtaposed than they are in extended chromatin.