Cryo-EM single-particle analysis expanding towards increasingly native samples

Cryo-EM single-particle analysis has revolutionized structural biology by allowing high-resolution analysis of large molecular assemblies that are not amenable to crystallography or NMR. Combination of this technology with innovative sample-preparation protocols further expands the range of potential targets.

Reconstructing biological molecules with help from video gamers

The results of the Foldit citizen science puzzles for crystallographic models and their integration into the PDB-REDO databank are discussed.

Critical evaluation of three cryo-EM structures of particulate methane monooxygenase by quantum refinement

We have studied the copper sites in three cryogenic electron-microscopy structures of particulate methane monooxygenase with quantum refinement. We show that the Cu_A, Cu_C and Cu_D sites are correctly modelled and that the Cu_B site is mononuclear in all structures, whereas we find no support for copper in the suggested trinuclear active site or two sites in the so-called copper sponge in PDB entry 7ev9.

Rescaling FSC curves

Calculating and plotting FSC curves on a uniform scale in inverse cubic resolution (Å⁻³) has several useful features.

Crystallographic fragment screening against SARS-CoV-2 nonstructural protein 1 using the F2X-Entry Screen and a newly developed fragment library

Two crystallographic fragment screening campaigns against SARS-CoV-2 nonstructural protein 1 resulted in the identification of 21 new hits.

Structural studies of NAD⁺-dependent methanol de­hydrogenase 1 from Bacillus methanolicus MGA3

The crystal structure of NAD⁺-dependent methanol dehydrogenase 1 from B. methanolicus MGA3 was determined at 3.0 Å resolution, revealing a decameric assembly, a Rossmann-fold coenzyme-binding site and Mn²⁺-dependent catalytic activity.