Protein structure can be determined by X-ray diffraction using a single diffraction image
Protein structures can theoretically be determined from single-molecule diffraction images using intense X-ray pulses and oversampling methods to solve the phase problem.
The claim refers to determining protein structure via X-ray diffraction using single diffraction images or single molecules (often explored via XFELs and oversampling/iterative phasing). Papers [10] and [11] explicitly support the feasibility of solving the phase problem and determining 3D structures from single-molecule or noncrystalline diffraction patterns using ultrashort X-ray pulses and oversampling.
Jianwei Miao, Henry N Chapman, Janos Kirz, David Sayre, Keith O Hodgson. Taking X-ray diffraction to the limit: macromolecular structures from femtosecond X-ray pulses and diffraction microscopy of cells with synchrotron radiation.. 2004. https://doi.org/10.1146/annurev.biophys.33.110502.140405
Discusses how continuous diffraction patterns from single noncrystalline specimens can solve the phase problem using the oversampling method.
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J Miao, K O Hodgson, D Sayre. An approach to three-dimensional structures of biomolecules by using single-molecule diffraction images.. 2001. https://doi.org/10.1073/pnas.111083998
Demonstrates that 3D structural determination of macromolecules can be achieved by combining ultrashort x-ray pulses for single-molecule diffraction with direct phase retrieval.
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