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Biophys J 92, 1439\u20131456 (2007).","journal-title":"Biophys J"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/j.bios.2014.11.025","article-title":"SPRi determination of inter-peptide interaction by using 3D supramolecular co-assembly polyrotaxane film","volume":"66","author":"Wang Y","year":"2015","unstructured":"Y Wang, , SPRi determination of inter-peptide interaction by using 3D supramolecular co-assembly polyrotaxane film. Biosens Bioelectron 66, 338\u2013344 (2015).","journal-title":"Biosens Bioelectron"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski Z","year":"1997","unstructured":"Z Otwinowski, W Minor, Processing of X-ray diffraction data collected in oscillation mode. 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