High-pressure macromolecular crystallography as a tool for studying protein flexibility

Lieske, J.; Saouane, S.; Reinke, P.Y.A.; Falke, S.; Ewert, W.; Meyer, J.; Pakendorf, T.; Burkhardt, A.; Crosas, E.; Hakanpää, J.; Stachnik, K.; Sieg, J.; Rarey, M.; Aßmann, M.; Zaun, H.; Kuballa, J.; Selikhanov, G.K.; Gabdulkhakov, A.G.; Chapman, H.N.; Günther, S.; Meents, A.

doi:10.1107/S2052252526008468

Figure 6
Pressure-induced movements in SARS-CoV-2 M^pro. (a) C_α—C_α DDM between the SARS-CoV-2 M^pro structures at atmospheric pressure and at 104 MPa. Crystal contacts of the HP structure are indicated as a green line pattern. One chain of the dimer contains 305 residues. Indicated are all crystallography-related interfacing residues according to PISA (Krissinel & Henrick, 2007

). (b) Depiction of the observed rotation of the N-terminal domain (1.1°) and the C-terminal domain (0.6°) of M^pro at 104 MPa (pink) compared with atmospheric pressure (green). The structures are superimposed on the rigid parts of the central β-sheet at the dimer interface.

IUCrJ

Volume 13| Part 6| November 2026|

ISSN: 2052-2525

https://doi.org/10.1107/S2052252526008468

BIOLOGY | MEDICINE

Open

access