@article{oai:repo.qst.go.jp:00085671,
 author = {Yunoki, Yasuhiro and Matsumoto, Atsushi and Morishima, Ken and Martel, Anne and Porcar, Lionel and Sato, Nobuhiro and Yogo, Rina and Tominaga, Taiki and Inoue, Rintaro and Maho, Yagi-Utsumi and Okuda, Aya and Shimizu, Masahiro and Urade, Reiko and Terauchi, Kazuki and Kono, Hidetoshi and Yagi, Hirokazu and Kato, Koichi and Sugiyama, Masaaki and Atsushi, Matsumoto and Hidetoshi, Kono},
 journal = {Communications Biology},
 month = {Mar},
 note = {In the cyanobacterial circadian clock system, KaiA, KaiB and KaiC periodically assemble into a large complex. Here we determined the overall structure of their fully assembled complex by integrating experimental and computational approaches. Small-angle X-ray and inverse contrast matching small-angle neutron scatterings coupled with size-exclusion chromatography provided constraints to highlight the spatial arrangements of the N-terminal domains of KaiA, which were not resolved in the previous structural analyses. Computationally built 20 million structural models of the complex were screened out utilizing the constrains and then subjected to molecular dynamics simulations to examine their stabilities. The final model suggests that, despite large fluctuation of the KaiA N-terminal domains, their preferential positionings mask the hydrophobic surface of the KaiA C-terminal domain, hindering additional KaiA-KaiC interactions. Thus, our integrative approach provides a useful tool to resolve large complex structures harboring dynamically fluctuating domains.},
 title = {Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach},
 volume = {5},
 year = {2022}
}