Thin sections of thc rachis of rcgcncrating follicles of pigmented fowl feathers and of maturc non-pigmcntcd seagull fcathcr rachis, cmbcddcd in mcthacrylatc and Aralditc rcspcctivcly, wcrc studicd in thc electron microscopc. Thc late stagcs of development of keratin fibrils wcrc cxamincd in OsO4-fixcd follicle matcrial, and aftcr poststaining with icad hydroxide the kcratin aggrcgatcs wcrc found to bc composed of finc microfibrils approximatcly 3 ° A in diamctcr apparently cmbcddcd in a matrix matcrial which had absorbed thc Icad stain. The centre-to-centre scparation of thc microfibrils was of the ordcr of 35 A. Aftcr bulk trcatmcnt by reduction with thioglycollic acid, OsO~ staining, and poststaining with Icad hydroxide, a similar microfibrillar finc structurc was obscrvcd in mature rachis. Only aftcr Icad staining could the microfibrils bc dclincatcd, and their diameter and separation wcrc similar to that found in thc keratin of thc follicle. It is suggcstcd that fcathcr keratin rcscmblcs c~-kcratins in consisting of microfibrils cmbcddcd in an amorphous protein matrix. However, in comparison with cz-kcratins, the microfibrils are much smaller in diamctcr, their arrangcment is less orderly, and on the basis of the rcactions towards the clcctron staining proccdures, the cystinc content of the matrix appears to bc not greatly differcnt from that of the microfibrils. Thc significance of a microfibrillar constitution of feather keratin is discussed in relation to currcnt structural modcls for this fibrous protein dcduccd from x-ray diffraction studies. The boundaries bctwccn thc component cells of fcathcr rachis arc dcsmosomal in character and similar to thosc of related kcratinous structures and a numbcr of different typcs of cells; the melanin granulcs arc dissimilar to thosc of mammalian epidermis in thcir apparcnt lack of mclanin-protein lamcllac.