Detection of Protein Assemblies in Crystals

The paper describes a new approach to the prediction of probable biological units from protein structures obtained by means of protein crystallography. The method first employs graph-theoretical technique in order to find all possible assemblies in crystal. In second step, found assemblies are analysed for chemical stability and only stable oligomers are left as a potential solution. We also discuss theoretical models for the assessment of protein affinity and entropy loss on complex formation, used in stability analysis.