Static compression is a useful tool to investigate the materials properties and phase behavior both under uniaxial stress and hydrostatic pressure. From evaluation of the equation of state（P-V-T relationship）to a discovery of near-room temperature superconductivity, the use of diamond anvil cells（DAC）and large-volume presses（LVP）as devices for static compression experiments that couple with synchrotron-based X-ray diffraction, spectroscopy, and imaging techniques achieved pioneering, paradigm-defining scientific advancements in multidisciplinary fields for the past two decades. High-Pressure Collaborative Access Team（HPCAT）is a sector at the Advanced Photon Source dedicated to developing multiple synchrotron-based X-ray techniques to maximize the utility of DAC and portable-LVP techniques to advance compression science. The beamlines are optimized to adapt various sample environments under extreme P-T conditions. HPCAT is comprised of two insertion device beamlines, one for diffraction and the other for spectroscopy, and two bending magnet beamlines, one for general purpose and the other for white-beam application, respectively. Each beamline’s specification and applications are introduced.
Protein crystallography has elucidated the structures of proteins, thereby deepening our understanding of life phenomena. Not only simple protein molecules but also protein assemblies can be subjected to crystal structure analysis. Subatomic resolution crystallography and time-resolved structure analysis make further contributions to life science. On the other hand, cryo-electron microscopy（cryo-EM）single-particle analysis has been successfully applied to structure determination of biological macromolecular assemblies. An advantage of protein crystallography is the high accuracy of the determined structure. Elucidation of the chemistry or physics of a protein molecule using its accurate structure is an important goal of protein crystallography that contributes greatly to progress in life science.