Research Interests
Our laboratory is dedicated to investigating the molecular mechanisms of biological macromolecules, with a specific focus on membrane proteins and protein-DNA complexes. We employ a multidisciplinary approach that encompasses various techniques such as X-ray crystallography, cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), biochemistry, and electrophysiology.
In addition to our studies on fundamental biological processes, we are actively involved in the development of new methods in the fields of single-particle cryo-EM and cryo-ET. By tackling recurring challenges and expanding the applications of these techniques, we aim to contribute to their continuous improvement and advancement.
Our Research
Cryo-EM structure of TMEM63C
TMEM63C exists primarily as a monomer under physiological conditions, in contrast, TMEM63B is a mix of monomer and dimer in cells, suggesting that oligomerization is a regulatory mechanism for TMEM63 proteins.
Cryo-EM structure of cyanophage P-SCSP1u
Our group reports the cryo-EM structure of the cyanophage P-SCSP1u, an MPP-C phages, in its native form at near-atomic resolution, which reveals the assembly mechanism of the capsid and molecular interaction of the portal-tail complex.
Neutralization Mechanism of Antibody again SARS-CoV-2
Cryo-EM analysis demonstrates that ZCB11 heavy chain predominantly interacts with Omicron spike trimer with receptor-binding domain in up conformation blocking ACE2 binding.
Cryo-EM structure of human pre-replication complex
The hMCM-DH with a constricted central channel untwists and stretches the DNA strands such that almost a half turn of the bound duplex DNA is distorted with 1 base pair completely separated, generating an initial open structure (IOS) at the hexamer junction.