Polyomaviruses are small, non enveloped, dsDNA viruses. Their capsids are formed by major capsid protein (VP1) and two minor capsid proteins (VP2 and VP3). Merkel cell polyomavirus (MCPyV) is a human pathogen form the family Polyomaviridae. MCPyV is widespread in humans and causes rare but aggressive skin tumors - Merkel cell carcinomas, in immunosuppressed individuals. No vaccines or antivirals against MCPyV are known. We determined the structure of the MCPyV virus like particle (VLP) by cryo-electron microscopy and single particle analysis to the resolution of 3.7 Å. Previously, structure of MCPyV VP1 pentamer, truncated from C and N terminus, was solved. Our reconstruction of whole VLPs reveals how pentamers form the capsid through interactions of C- and N-terminal parts of VP1s. Capsid stability is strengthened by disulfide bonds between VP1s from two adjacent pentamers.