Although experimental protein-structure determination usually targets known proteins, chains of unknown sequence are often encountered. They can be purified from natural sources, appear as an unexpected fragment of a well characterized protein or appear as a contaminant. Regardless of the source of the problem, the unknown protein always requires characterization. Here, an automated pipeline is presented for the identification of protein sequences from cryo-EM reconstructions and crystallographic data. The method's application to characterize the crystal structure of an unknown protein purified from a snake venom is presented. It is also shown that the approach can be successfully applied to the identification of protein sequences and validation of sequence assignments in cryo-EM protein structures.

The genus Akodon is one of the most species-rich rodent lineages in South America. In Peru, this genus contains 14 species subdivided in two groups: aerosus and boliviensis. Akodon orophilus Osgood, 1913 (Rodentia: Cricetidae) is a member of the Akodon aerosus group that inhabits the northern Peruvian montane forest, but is poorly characterized and its distri-bution is vaguely known. We review the status of the species based on morphology, morphometric and karyology, and compared with all members of the Akodon aerosus clade from Peruvian montane forests. As a result, we provide a com-plete redescription of A. orophilus, present new information on its natural history, restrict its distribution to the east of Río Marañón, and describe a new species of Akodon from Huánuco Department, central Peru, a population previously as-signed to A. orophilus.