In a paper published online on 12 August 2026, Paknia and colleagues reported a 0.43 Å structure of Pyrococcus abyssi rubredoxin, which they described, “to the best of our knowledge,” as the highest-resolution protein structure yet determined. The result depended on an unusually large, well-ordered crystal, carefully controlled synchrotron data collection and an electron-density model that could represent bonding electrons.
What does the reported resolution mean?
An ångström (Å) is one ten-billionth of a metre. In crystallography, a smaller resolution value indicates that the diffraction data can distinguish finer spatial detail. But a single headline number does not describe how evenly that detail was measured in every direction.
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For the rubredoxin dataset, Paknia et al. reported directional diffraction limits of 0.441, 0.462 and 0.456 Å, with an overall stated resolution range of 26.62–0.433 Å. The diffraction cutoff was anisotropic: the data did not extend equally far in all directions. The paper therefore reports different completeness figures depending on the cutoff shape—96.2% for an ellipsoidal cutoff and 84.4% for a spherical one. In the highest-resolution shell, those figures were 59.9% and 22.3%, respectively.
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How did the experiment reach such fine detail?
The approach combined a large cryocooled crystal with a beam matched to its dimensions, low-dose collection, data gathered at multiple orientations and a detector suited to high-energy X-rays. No single component accounts for the result; the experimental strategy was designed to collect extensive diffraction data while preserving useful crystal order.
A large, carefully prepared crystal
The investigators studied a W4L, R5S variant of rubredoxin from P. abyssi. They grew crystals by sitting-drop vapour diffusion in concentrated sodium malonate, then cryo-cooled the crystal directly in liquid nitrogen. The crystal used for diffraction was approximately 600 × 500 × 300 μm and was mounted in a MiTeGen Dual Thickness MicroLoop.
In discussing very high-resolution work, the authors emphasize exceptionally well-ordered crystals, reproducible sample quality and cryogenic collection. They report that their experience suggests crystals exceeding 250 μm in each dimension are desirable for reproducible sub-ångström data collection, and that resolutions of 0.5–0.7 Å or better typically require very low average B factors. These are the authors’ reported experience and guidance, not universal thresholds for every protein or beamline.
A uniform beam and multiple orientations
Data were collected at 100 K on EMBL Hamburg’s P14 beamline at DESY’s PETRA III storage ring. The X-ray energy was 32.142 keV, corresponding to a wavelength of 0.3857 Å. A 601 × 507 μm top-hat beam—slightly larger than the crystal—provided relatively homogeneous illumination across it. In this context, “top-hat” describes a beam with a broad, flat illumination profile rather than a strongly peaked intensity distribution.
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The team used a multi-orientation collection strategy to improve reciprocal-space coverage while managing geometric constraints and shadowing. An automated workflow characterized the crystal, planned collection orientations and coordinated data processing. Diffraction was recorded with a DECTRIS EIGER2 CdTe 16M detector.
Managing radiation damage
X-rays can damage a crystal during measurement, potentially changing the sample and degrading the diffraction data. The researchers estimated the total absorbed dose for this collection at 500 kGy and describe low-dose strategy as important for reaching this level of detail. The paper does not make 500 kGy a general safe-dose limit; it is the estimated dose for this particular experiment.
The result illustrates a practical constraint: collecting enough high-quality diffraction data while limiting damage requires balancing exposure, crystal quality, orientation and coverage. A more intense beam by itself would not solve that problem.
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The study reports 6,545,565 total reflections and 245,905 unique reflections. Across the dataset, mean I/σ(I) was 23.9; in the highest-resolution shell it was 1.7. These statistics help describe the measurements alongside the directional resolution and the choice of completeness cutoff. They should not be treated as substitutes for assessing the refined model and the quality of its fit to the data.
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The paper’s distinction between spherical and ellipsoidal cutoffs is especially relevant: a reader comparing resolution statistics should check how anisotropy and completeness were handled, rather than comparing only the smallest quoted Å value.
Independent reader supportYour contribution helps us test, update, and keep practical guides available for everyone.Why did the researchers use an aspherical atom model?
Resolution can make fine electron-density features observable, but the model used to interpret that density also matters. The independent atom model (IAM), commonly used in crystallographic refinement, represents atoms with spherical scattering factors. In the rubredoxin study, difference maps from the IAM showed positive density around chemical-bond midpoints—features that a simple spherical-atom description does not represent well.
The researchers connected the DiSCaMB transferable aspherical atom model (TAAM) library to BUSTER. Unlike the spherical approximation, this aspherical model can represent deformation of electron density associated with chemical bonding. In refinement, TAAM resolved the bond-midpoint features as bonding-electron deformation density.
The authors report accurate nuclear positions, including hydrogen atoms, as well as electron-density observations such as bond-midpoint density and atomic partial charges. Those are findings from this rubredoxin structure. The authors also suggest that the methodology could support more routine quantum crystallography of biological macromolecules when accurate diffraction data are available; that broader routine use is a prospective implication, not something established by one structure.
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How does this compare with serial femtosecond crystallography?
The 0.43 Å rubredoxin structure was collected at a synchrotron using a cryocooled crystal and a low-dose strategy. Serial femtosecond crystallography (SFX) at an X-ray free-electron laser (XFEL) is a different approach, suited to different sample and research constraints. The methods should not be conflated: “diffraction before destruction” describes the use of ultrashort XFEL pulses to collect diffraction before major damage processes take hold, not the method used for this record.
| Approach | Useful context | Strength | Trade-off or limit |
|---|---|---|---|
| Low-dose synchrotron macromolecular crystallography | A sufficiently large, well-ordered crystal and a goal of high static structural detail. | The rubredoxin study combined cryogenic collection, a crystal-matched top-hat beam, low-dose planning and multiple orientations. | Requires unusually high crystal quality and size; radiation damage remains a constraint on dose and collection. |
| Serial femtosecond crystallography at an XFEL | Small crystals, room-temperature measurements or fast and irreversible dynamics. | Ultrashort intense pulses can collect diffraction before many damage processes occur; fresh crystals are supplied serially. | Each crystal is ultimately destroyed, so the method needs many crystals and crystal-delivery and processing infrastructure. It was not used for the rubredoxin structure. |
A 2019 IUCr review discusses both the ability of XFEL pulses to outrun many damage processes and evidence that some damage can still occur, along with mitigation needs. European XFEL describes SFX applications including small crystals and time-resolved work.
How rare is sub-ångström protein crystallography?
Sub-ångström structures remain exceptional rather than routine. Paknia et al. counted 20 PDB entries in the 0.5–0.7 Å range as of 9 May 2026: 15 protein structures, four Z-DNA structures and one RNA structure. That dated count is a snapshot of entries in that range; it is not a count of all structures at or below 0.7 Å after the rubredoxin paper.
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