Journal Article

PUBDB-2026-02440

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png High-pressure macromolecular crystallography as a tool for studying protein flexibility

Lieske, J.CFEL*Extern*XFEL.EU*DESY* ; Saouane, S.Extern*DESY* ; Reinke, P.CFEL*DESY* ; Falke, S.CFEL*Extern*EMBL*DESY* ; Ewert, W.CFEL*EMBL*DESY* ; Meyer, J.CFEL*XFEL.EU*DESY* ; Pakendorf, T.CFEL*XFEL.EU*DESY* ; Burkhardt, A.XFEL.EU*DESY* ; Crosas Ubeda, E.EMBL*DESY* ; Hakanpaeae, J.DESY* ; Stachnik, K.Extern* ; Sieg, J. ; Rarey, M. ; Assmann, M.Extern* ; Zaun, H.Extern* ; Kuballa, J. ; Selikhanov, G.Extern*XFEL.EU* ; Gabdulkhakov, A.Extern*EMBL* ; Chapman, H. N.CFEL*XFEL.EU*DESY* ; Guenther, S.CFEL*XFEL.EU*DESY* ; Meents, A. (Corresponding author)CFEL*XFEL.EU*DESY*

2026
[Verlag nicht ermittelbar] Chester

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Please use a persistent id in citations: doi:10.1107/S2052252526008468

Abstract: Protein function depends on their conformational flexibility. Complementary to temperature-dependent studies, high-pressure (HP) macromolecular crystallography is well suited to explore the conformational space of proteins at atomic resolution. We have developed a new HP cell concept for macromolecular X-ray crystallography overcoming 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 (HP). 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.

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Contributing Institute(s):

1. FS-CFEL-1 Fachgruppe BMX (FS-CFEL-1-BMX)
2. Innovation und Technologietransfer (ITT)
3. Coherent Imaging (CFEL-I)
4. PETRA-D (FS-PETRA-D)
5. DOOR-User (DOOR)

Research Program(s):

1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)
2. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
3. FISCOV - FISCOV Helmholtz large research infrastructures in the fight against epidemic outbreaks (FISCOV) (FISCOV)
4. InternLabs-0011 - HIR3X - Helmholtz International Laboratory on Reliability, Repetition, Results at the most advanced X-ray Sources (2020_InternLabs-0011) (2020_InternLabs-0011)
5. FS-Proposal: I-20181059 (I-20181059) (I-20181059)
6. FS-Proposal: II-20190007 (II-20190007) (II-20190007)
7. FS-Proposal: I-20191472 (I-20191472) (I-20191472)

Experiment(s):

1. PETRA Beamline P11 (PETRA III)

Appears in the scientific report 2026

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