In the framework of transnational collaborations within the EU BIOMED program,
we have started crystallographic work on apolipoprotein A-I and on
HIV-regulating proteins. Furthermore, we are trying to improve the
understanding of protein crystallization by means of a systematic analysis of
protein solubilities. So far, a practical result of this work has been the
development of specific two-component-systems (e.g., PEG & NaCl) which allow a
rational approach to the crystallization of proteins. As an extension of our
work with 4-á-helix bundles, we are developing novel sequence-alignments
techniques which are specifically designed to yield statistically significant
local alignments between sequences. In the case of proteins, the relationship
between the significance of the resulting alignments and structural similarity
is under investigation. The aim is to develop a powerful, user-friendly program
for the alignment of nucleic acid or protein sequences, which can conveniently
interact with existing program suites for sequence analysis.
