Laboratory of Protein Crystallography


Professor Genji KURISU
Associate Prof. Hideaki TANAKA
Specially Appointed Assistant Prof. Christoph GERLE
Assistant Prof. Tetsuko NAKANIWA
Technical Staff  Naoko NORIOKA



Tel 81-6-6879-8604
Fax 81-6-6879-8606


In the 1959 the division of Protein Crystallography was established to elucidate the molecular structure of proteins by X-ray crystal structure analysis. The X-ray method has become the most powerful tool to determine protein structure. One of our aims is to spread the application of this method throughout biological science. Our own research targets are focused on biological macromolecular assemblies and membrane proteins. All of these are long term and important projects.

Fig.1. Crystal structure of the electron transfer complex between Ferredoxin and Photosytem I. Moving gif side view images of one protomer from the complex with/without Fd are shown. Bound Fd molecule is shown in cyan (Nature Plants 4, 218-224, 2018)
Fig. 2: Overall structure of the cytoplasmic dynein motor domain depicted with the model of a microtubule.The force-generating rod-like linker, the ATP-hydrolyzing ring and the dynein specific C-sequence units are located sequentially from the N-terminus. Characteristic Y-shaped structure called “stalk and strut coiled-coils” are inserted into the AAA4 and AAA5 modules (Nature 484, 345-350, 2012).


Fig. 3: Crystal structure of the hetero-tetrameric catalytic component NB-protein of DPOR (Dark-operative Protochlorophyllide OxidoReductase). The [4Fe-4S] clusters are shown in CPK model, and the Pchlide molecules in stick model. The BchN and BchB subunits in one dimer are colored in green and blue (Nature 456, 110-114, 2010).

Current Research Programs

  1. Structural studies of photosynthetic energy-transducing membrane and related redox enzymes
  2. Crystal structure analyses of dynein motors
  3. High resolution structural analysis of rat liver vault


  1. X-ray structure of an assymetrical trimeric ferredoxin-photosystem I complex. Kubota-Kawai, H. et al., (2018) Nature Plants 4, 218-224
  2. Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast.> Hochmal, A.K. et al., (2016) Nature Commun., 7, 11847
  3. The 2.8Å crystal structure of the dynein motor domain. Kon, T. et al., (2012) Nature 484, 345-350
  4. X-ray crystal structure of the light-independent protochlorophyllide reductase. Muraki, N. et al., (2010) Nature 465, 110-114
  5. The Structure of Rat Liver Vault at 3.5 Angstrom Resolution. Tanaka, H. et al., (2009) Science 323, 384-388