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Abstract
The structure of Langmuir lysozyme films on a liquid surface, formed from crystallization solutions with addition of metal chlorides as a precipitant, have been investigated. The thicknesses and densities of the films were determined using the X-ray reflectivity technique, and the concentration distribution profiles of the sulfur atoms present in protein molecules, as well as precipitant ions in the subphase surface region, have been obtained by the X-ray standing waves technique. Based on the experimental results, the dependence of the film structure on the precipitant used, as well as some specific features of application of X-ray reflectivity and X-ray standing waves techniques in the study of Langmuir films of globular proteins on a liquid surface, are analyzed.
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