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E"},{"key":"10.1016\/j.tcb.2020.08.007_bb0565","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1110\/ps.041148605","article-title":"A voyage to the inner space of cells","volume":"14","author":"Baumeister","year":"2005","journal-title":"Protein Sci."},{"key":"10.1016\/j.tcb.2020.08.007_bb0570","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.copbio.2009.03.008","article-title":"Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes","volume":"20","author":"Plitzko","year":"2009","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.tcb.2020.08.007_bb0575","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/j.bpj.2015.10.053","article-title":"Site-specific cryo-focused ion beam sample preparation guided by 3D correlative microscopy","volume":"110","author":"Arnold","year":"2016","journal-title":"Biophys. 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