The bacterium Lysobacter species strain XL1 is known as a producer of extracellular lytic enzymes, which are capable of degrading cell wall components of other bacteria and simple eukaryotes. This ability determines the ecological, medical and agricultural relevance of Lysobacter sp. XL1. However, the molecular mechanism of secretion of lytic exoenzymes from Lysobacter cells is yet unknown, which in turn necessitates the search of protein-protein interactions that occur during exoenzyme secretion. The current paper is concerned with investigation of protein complexes that are likely formed during the secretion of AlpB lytic protease from the cells of Lysobacter sp. XL1. In this study, we have optimized the method of stabilization of protein complexes formed in the intact cells of Lysobacter sp. XL1 by using crosslinking reagent dithiobis(succinimidylpropionate) (DSP) and detected DSP-linked protein complexes by the monoclonal antibodies against AlpB propeptide. © 2013 Elsevier Ltd. All rights reserved.