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X-ray crystallography 
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A combination of X-ray diffraction analysis, spectroscopic methods,
computational chemistry methods, molecular computer graphics, and bioassays is
applied to study biologically active molecules and their complexes with the
proteins-“receptors”. The phytohormone auxin family, e.g. natural growth
promoters, and their synthetic analogues are studied since a minor structural
modification may result in a growth inhibitor (antiauxin). A classification of
auxin growth regulators is proposed and it will be important tool in design and
production of new agrochemicals. The mechanism of biocatalytic activity of
bacterial lipases is also studied using interdisciplinary approache.
Enantioselectivity of Burkholderia cepacia lipase towards a wide range of
secondary alcohols is evaluated using molecular modeling and chemometric
analysis. A novel lipase from Streptomyces rimosus is isolated, cloned
and biochemically characterized. The enzyme is structurally characterized by
MALDI mass spectrometry. Another area of research is the topology of hydrogen
bonding and its function in design of new nanohedral materials.