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Publication Abstract from PubMed

Recent advances in 3D electron diffraction have allowed the structure determination of several model proteins from submicrometric crystals, the unit-cell parameters and structures of which could be immediately validated by known models previously obtained by X-ray crystallography. Here, the first new protein structure determined by 3D electron diffraction data is presented: a previously unobserved polymorph of hen egg-white lysozyme. This form, with unit-cell parameters a = 31.9, b = 54.4, c = 71.8 A, beta = 98.8 degrees , grows as needle-shaped submicrometric crystals simply by vapor diffusion starting from previously reported crystallization conditions. Remarkably, the data were collected using a low-dose stepwise experimental setup consisting of a precession-assisted nanobeam of approximately 150 nm, which has never previously been applied for solving protein structures. The crystal structure was additionally validated using X-ray synchrotron-radiation sources by both powder diffraction and single-crystal micro-diffraction. 3D electron diffraction can be used for the structural characterization of submicrometric macromolecular crystals and is able to identify novel protein polymorphs that are hardly visible in conventional X-ray diffraction experiments. Additionally, the analysis, which was performed on both nanocrystals and microcrystals from the same crystallization drop, suggests that an integrated view from 3D electron diffraction and X-ray microfocus diffraction can be applied to obtain insights into the molecular dynamics during protein crystal growth.

Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme.,Lanza A, Margheritis E, Mugnaioli E, Cappello V, Garau G, Gemmi M IUCrJ. 2019 Jan 15;6(Pt 2):178-188. doi: 10.1107/S2052252518017657. eCollection, 2019 Mar 1. PMID:30867915^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.