Two-dimensional arrays of streptavidin bound to a biotinylated polymer monolayer at the air-water interface were studies by polarized fluorescence microscopy and X-ray reflectivity. Domains with long-range orientational order were observed. These could be reversibly deformed and compressed, changing their area by a factor of 2 without destroying positional order. In accordance with this, X-ray reflectivity revealed changes in electron density proving that water was squeezed out of the protein domains. The high compressibility suggested liquid crystalline instead of crystalline order within the protein domains.