Midterm ReviewProtein Crystallography Research Group
Date: June 2011 (conducted by e-mail)Reviewers:- Dr. Yu-Shan Huang, Head of the Taiwan Beamline Office, NationalSynchrotron Radiation Research Center- Dr. Masaki Takata, Deputy Director, RIKEN SPring-8 Center-

Dr. Yoshitsugu Shiro, Deputy Director, RIKEN SPring-8 Center
Dr. Masaki Yamamoto, Director of Advanced Photon Technology Division,RIKEN SPring-8 Center

General Comments:[Reviewer 1]
The information provided in the carefully preparatory documents is clear
enough and allows the reviewer a detailed review of the PXRG performance.
In brief, the overall appraisal of the level and quality of the PXRG’s research
activity is EXCELLENT* according to its quality and quantity ofpublications as well as its great contributions to the structural biology
society. The overall appraisal of the level and quality of the PXRG’smanagement is EXCELLENT* according to an efficient management provedby its solid research directions, very convincing results with limited
manpower, international collaboration and industrial application, andgrowing funding from various sources. The reviewer is therefore sure that
the PXRG’s major group mission, being support for users both in-house andoutside, has been very successfully executed.
*poor = 0-2, fair = 3-4, good = 5-6, excellent =7-9
[Reviewer 2]
The RSC Protein Crystallography Research Group (PCRG) is achieved an
important mission by continuing and further developing the activities of thenational structural genomics project of Japan’s “Protein 3000” initiative (FY2002-2006) and successfully took over the resources and functions of theHigh Through-Put Factory (HTPF) to launch the Protein Tectonics Platform(PTP) as an integrated research infrastructure for protein crystallography inthe SPring-8. As a result, the PTP promoted fruitful international
collaboration with Taiwan NSRRC in addition to the basic infrastructuralrole for structural biology research at RIKEN SPring-8 Center (RSC).
In the RSC as a world-leading Photon Science Research Complex with theSPring-8 and SACLA, the area of the PCRG’s activities, however, shall betransferred from the structural biology based on the crystallography to thephoton control science, which allow an advanced visualization and/orcreation of biological function such as “Bio-function photon science”. Since
this movement is the common with the trend of the materials science in RSC,
the PCRG may be expected to cover the whole research area relating to thephoton science. It is, therefore, the strategy concept and positioning of thePCRG in the Advanced Photon Technology Division should be reviewed andenhanced to facilitate activities of the newly-emerged RSC with SPring-8and SACLA.
[Reviewer 3]This Group started in 2008, which was based on the facilities and theresearch achievements of the national projects “Protein 3000” in theSPring-8 site. The “Protein 3000” was the big national project, the purposeof which was determination of 3000 protein structures by X-ray
crystallographic and NMR techniques.
To pursue the purpose, newfacilities were launched and new technologies were developed. It is highly
appreciated that the Group was established at the SPring-8 site after
completion of the project, in order to broaden the achievement of the projectto the general users of SPring-8 who are interested in structural biology. In
the first 3 years, the group appeared to make efforts to establish the facilities
and management systems, and is now settled down for its activities.
[Reviewer 4]
1. Present status of RSC Protein Crystallography Research Group
RSC Protein Crystallography Research Group (PCRG) was established as
the successor to the High Through-Put Factory (HTPF) prepared by thenational structural genomics project of Japan’s “Protein 3000” initiative (FY2002-2006). A vast of resources took over the HTPF were rearranged to theProtein Tectonics Platform (PTP) as a research infrastructure for protein
crystallography in the SPring-8 campus. The PCRG steadily operate the PTP

in spite of the limited human resources. The PTP has been playing theimportant role as the basic infrastructures for structural biology research at
RIKEN SPring-8 Center (RSC) and the international collaboration with
Taiwan NSRRC.
PCRG has developed various technologies for the protein crystalengineering. A novel protein crystallization method using microporous
zeolite as a heteroepitaxic nucleant is a unique and a promising technology
to standardize the process of protein crystallization. More practicalexperiments to crystallize the structure unknown proteins will be strongly
expected. A crystal contact design to improve diffraction quality of protein
crystals by introducing mutations is an interesting study to improve thequality of the structure known crystals. In order to generalize this idea, morepractical case studies will be recommended.
2. Future prospects for RSC biological research
PCRG are making important efforts for basic protein crystallography
research at RSC. However, many types of equipment at the PTP are mainly
focused on the High Through-Put protein crystallography for statistic
structures of soluble proteins. Today’s PTP based on the infrastructure
prepared by “Protein 3000” before 2006 has been losing the competitive
power in modern protein research according to the aging and changing thedirection of protein science.
The leading edge targets of biological and protein science are moving fromsoluble proteins to membrane proteins and from statistic structures todynamical structures according to the progress of the instrumentation andmethods of SR and XFEL. At the SPring-8 campus, micro-focused X-rays at
RIKEN Targeted protein beamline and X-ray Laser at SACLA have beenutilized recently. Those will open the next door for biological and proteinscience. In order to accelerate and support the cutting-edge biological scienceat the SPring-8 campus, next generation infrastructures for biologicalresearch targeted not only proteins including membrane proteins but also
higher order biological samples; for example, cell, cell organelle and supra
molecule complexes, are strongly expected.