9TLI
Horse hemoglobin structure from serial crystallography with 3 fs pulse
Summary for 9TLI
| Entry DOI | 10.2210/pdb9tli/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total) |
| Functional Keywords | hemoglobin, radiation damage, hem protein, metal binding, oxygen binding |
| Biological source | Equus caballus (horse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 65257.01 |
| Authors | Sprenger, J.,Oberthuer, D.,Galchenkova, M.,Yefanov, O.,Metz, M.,Sarrou, I.,Caleman, C. (deposition date: 2025-12-10, release date: 2026-10-14) |
| Primary citation | Galchenkova, M.,Dawod, I.,Cardoch, S.,Sprenger, J.,Oberthur, D.,Awel, S.,De Santis, E.,Granas, O.,Knoska, J.,Metz, M.,Passmore, S.,Pena, G.,Sarrou, I.,Wiedorn, M.,Timneanu, N.,Chapman, H.,Yefanov, O.,Caleman, C. Radiation damage in serial femtosecond crystallography studied in hemoglobin. Acta Crystallogr D Struct Biol, 82:1169-1180, 2026 Cited by PubMed Abstract: A central question in macromolecular crystallography is what X-ray free-electron laser pulse duration is required to obtain damage-free structural information. We compare serial femtosecond crystallography data from hemoglobin crystals using 3 and 10 fs pulses at comparable peak intensities (∼3 × 10 W cm) and fixed photon energy (7.15 keV). Structural refinement produced very similar models and resolution-dependent data-quality indicators remained comparable. Both datasets also retained sufficient anomalous signal for phasing. These observations support the conclusion that high-resolution scattering was preserved under both pulse durations. Hybrid collisional-radiative and molecular-dynamics simulations show that under typical experimental conditions, atomic form-factor changes are negligible (<1%) and atomic displacements fall below the resolution limit imposed by the X-ray photon energy and the geometry of the detector. The combined experimental and theoretical results indicate that 10 fs pulses are adequate to obtain damage-free protein structures using femtosecond crystallography under the intensity conditions explored. PubMed: 42813594DOI: 10.1107/S2059798326008569 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.46 Å) |
Structure validation
Download full validation report
