Authors
Julia Lieske, Sofiane Saouane, Patrick Y A Reinke, Sven Falke, Wiebke Ewert, Jan Meyer, Tim Pakendorf, Anja Burkhardt, Eva Crosas, Johanna Hakanpää, Karolina Stachnik, Jochen Sieg, Matthias Rarey, Miriam Aßmann, Henning Zaun, Jürgen Kuballa, Georgii K Selikhanov, Azat G Gabdulkhakov, Henry N Chapman, Sebastian Günther, Alke Meents
Published in
IUCrJ. Nov 01, 2026. Epub Nov 01, 2026.
Abstract
Protein function depends on their conformational flexibility. Complementary to temperature-dependent studies, high-pressure (HP) macromolecular crystallography is well suited to exploring the conformational space of proteins at atomic resolution. We have developed a new HP cell concept for macromolecular X-ray crystallography that overcomes the limitations of current devices. It consists of a single-crystalline sapphire capillary, which is loaded with multiple crystals and pressurized with helium at freely adjustable gas pressures of up to 120 MPa. Studying five different proteins, we generally observed a compression of the protein structures and a decrease in thermal displacement parameters at high pressure. Structurally, observations included the compression of a central tunnel of a biotechnologically relevant enzyme and the stabilization of ligand binding in the membrane protein photosynthetic reaction center of Cereibacter sphaeroides. For two pharmaceutically relevant proteins, the human kinase DRAK2 and SARS-CoV-2 main protease, we identified concerted movements of subdomains. Such knowledge is essential for predictions of protein dynamics and defined conformational states, offering the potential for improved structure-based drug development.
PMID:
42895459
Bibliographic data and abstract were imported from PubMed on 19 Oct 2026.
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