issue contents

ISSN: 2052-2525

November 2022 issue

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editorial


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The 2022 meeting of the American Crystallographic Association in Portland was an inspiring event, addressing a range of both conventional and emerging themes in structural biology. The increasing emphasis at the conference on methods outside the conventional envelope of crystallography, especially cryo-electron microscopy, is discussed.

scientific commentaries


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Electron diffraction patterns unavoidably contain in-plane distortions introduced by electromagnetic lens systems. Geometric correction of different distortion types allows the accuracy of lattice parameter determination to be improved in 3D electron diffraction data.

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Commentary is given on a paper [Urzhumtsev & Lunin (2022). IUCrJ, 9, 728–734] proposing a new method for the analytic modelling of inhomogeneous resolution in electrostatic potential volumes and electron density maps for improved real-space refinement.

research letters


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Family-wide structural analyses of human TRIM NHL domains reveal evolutionary divergence of their β-propeller architecture that might be essential for recruiting diverse interacting partners and for the roles of NHL domains as E3 ligases.

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A decomposition of 3D oscillating functions results in analytic expressions for atomic model density maps distorted by inhomogeneous resolution and atomic positional disorder. Such decomposition extends the possibilities of real-space refinement of atomic models.

research papers


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Refinement of optical distortions in 3D electron diffraction data allows the determination of accurate lattice parameters and improves intensity integration.

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The use of room-temperature crystallography to probe protein dynamics on the second-to-minute timescale is demonstrated by monitoring the release of a photoequilibrium induced in crystals of a LOV domain. The slow protein dynamics components include the relaxation of a photoadduct and a crystalline phase transition. The result of the latter is the formation of a non-crystallographic dimer in which the C-termini of the two monomers reorder in distinct conformations on different timescales.

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Low-energy native-SAD phasing using a helium path could be used more routinely for solving challenging membrane protein structures.

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