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. 2016 Mar 9;6(3):150237. doi: 10.1098/rsob.150237

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© 2016 The Authors.

Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.

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Figure 1. — Isolation and architecture of monomeric Dam1 complex by cross-linking. (a) SDS–PAGE analysis of the Dam1 complex cross-linked with BS3. Cross-linked Dam1 complex was excised and analysed by mass spectrometry. Asterisk denotes that excluded from our analysis. (b) Fragmentation spectrum of a cross-linked peptide that includes a link between Lys-13 in Dad2 and Thr-2 in Spc19. Peaks supporting TDALEQSVLALEGTVSVLK are annotated in red, and those supporting KELQSLQK are annotated in blue. (c) Intersubunit and intramolecular cross-link maps for the monomeric Dam1 complex. Intramolecular and intermolecular cross-links are coloured purple and green, respectively. Predicted coiled coil regions are in light blue. (d) Representative EM map of the monomeric Dam1 complex (modified from EMDB: 1972), highlighting the reported positions of subunit termini in previous studies.