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. 2014 Mar 31;42(9):6038–6051. doi: 10.1093/nar/gku232

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© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Structure-based mutagenesis to disrupt the Vps75 tetramer. (A) Model of Vps75 tetramer, opposing Vps75 dimers in blue and green, with the positions of non-tetramerising mutants shown as colour-coded spheres matching SEC–MALS elution profiles of the corresponding mutant; K169E (grey), K170E (red) and R164D (black) compared to wild-type Vps75 (blue). (B) The location of K78 (yellow spheres) that was mutated to cysteine for disulphide cross-link formation to trap Vps75 in its tetrameric conformation and SEC–MALS analysis at 500 mM NaCl of Vps75 disulphide cross-linked at 150 mM NaCl via K78C.