We report on X-ray reflectivity and diffraction studies using monolaye
rs of phospholipids and of the protein streptavidin specifically bound
to monolayers. For phospholipids with the phosphocholine head group a
ttached to the glycerol backbone via (flexible) ethylene oxide spacers
, we demonstrate that the lateral interactions can be reduced by incre
asing of the spacer length. This is reflected in a reduction of the ti
lt angle of aliphatic tails. Diffraction of the protein layer can be o
bserved in situ. The data reveal that positional order is merely short
-ranged and that the structure can be changed reversibly via film comp
ression and expansion.