BDR researchers coming from diverse research fields are working together to achieve higher goals.

Seminars & Symposia

Seminars & Symposia

BDR hosts annual symposium and regular seminars inviting international scientists in life science.

Careers & Study

Careers & Study

BDR embraces people from diverse backgrounds, and strives to create an open and supportive setting for research.



BDR communicates the appeal and significance of our research to society through the use of various media and activities.



From research, events, people and everything in between, find out what’s going on at RIKEN BDR.

About Us

About Us

Exploring the scientific foundations of life through interdisciplinary approaches to address society’s problems.

Photo of Team leder, Mikako Shirouzu

Team Leader
Mikako Shirouzu Ph.D.

Laboratory for Protein Functional and Structural Biology



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Establishment of a structural analysis technology platform that contributes to "life innovation" such as drug development and medical treatment.

The high-resolution structural information of proteins related to diseases shall increasingly become important for drug development leading to future individualized medicine. We plan to establish a structural analysis technology platform to contribute to "Life innovation" such as drug discovery as well as development of methods for the sample preparation of challenging proteins including membrane proteins/biomolecular complexes and for the structural analysis by cryo-electron microscopy (cryo-EM). The 3D-structural information will be used for in-silico screening/design of chemical compounds and for dynamic structural analysis toward simulation research of cell function.

cryo-EM (FEI Tecnai Arctica)

Research Theme

  • Analysis of developmental process using theoretical cell models
  • Study of evolutionary dynamics of microorganisms by comprehensive phenotypic/genetic analysis
  • Development of algorithm for high-resolution comprehensive phenotypic/genetic analysis

Selected Publications

Yamagata A, Murata Y, Namba K, et al.
Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter.
Nature Communications 13, 7180 (2022) doi: 10.1038/s41467-022-34930-1

Ehara H, Kujirai T, Shirouzu M, et al.
Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.
Science 377(6611), eabp9466 (2022) doi: 10.1126/science.abp9466

Nakamura H, Hisano T, Rahman MM, et al.
Structural basis for heme detoxification by an ATP-binding cassette-type efflux pump in gram-positive pathogenic bacteria.
Proceedings of the National Academy of Sciences of the United States of America 119(27), e2123385119 (2022) doi: 10.1073/pnas.2123385119

Park JH, Iwamoto M, Yun JH, et al.
Structural insights into the HBV receptor and bile acid transporter NTCP.
Nature 606(7916), 1027-1031 (2022) doi: 10.1038/s41586-022-04857-0

Cao P, Bracun L, Yamagata A, et al.
Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.
Nature Communications 13, 1977 (2022) doi: 10.1038/s41467-022-29563-3

Hosaka T, Nomura T, Kubo M, et al.
Conformational alterations in unidirectional ion transport of a light-driven chloride pump revealed using X-ray free electron lasers.
Proceedings of the National Academy of Sciences of the United States of America 119(9), e2117433119 (2022) doi: 10.1073/pnas.2117433119

Nakagawa Y, Shen HC, Komi Y, et al.
Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system.
Nature Chemical Biology 18(3), 321-331 (2022) doi: 10.1038/s41589-021-00951-y

Shimizu K, Iyoda T, Sanpei A, et al.
Identification of TCR repertoires in functionally competent cytotoxic T cells cross-reactive to SARS-CoV-2.
Communications Biology 4, 1365 (2021) doi: 10.1038/s42003-021-02885-6

Kasahara K, Re S, Nawrocki G, et al.
Reduced Efficacy of a Src Kinase Inhibitor in Crowded Protein Solution.
Nature Communications 12, 4099 (2021) doi: 10.1038/s41467-021-24349-5

Kukimoto-Niino M, Katsura K, Kaushik R, et al.
Cryo-EM structure of the human ELMO1-DOCK5-Rac1 complex.
Science Advances 7(30), eabg3147 (2021) doi: 10.1126/sciadv.abg3147