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Leishamnia parasites are the causative agents of the leishmaniasis disease. Twenty species of Leishmania sp has been described as human pathogens and several of them present different clinical manifestations. There is no a protective vaccine for humans. Alternatives to discover new drugs are based on the design of new compounds that bind selected targets. Mainly, the targets are proteins involved in key metabolic or cellular processes of the pathogen, e.g. parasitization of vertebrate host cells. The parasitization of the vertebrate host by Leishmania parasites depends on the expression of different molecules including Lack protein. In this article we highlight the conditions to perform the refold, purification, and crystallizing of the Lack protein of the human pathogen Leishmania (Viannia) panamensis. Moreover, we present structure modelling analysis, the structure of Lack protein was found to be similar to RACK1-ribosome associated protein from Trypanosoma brucei and Saccharomyces cerevisiae and other eukaryotes. The structural characteristics of Lack protein could be used for exploration of new drugs. [ABSTRACT FROM AUTHOR]