On the application of the expected log-likelihood gain to decision making in molecular replacement

The expected log-likelihood gain can be used to predict the outcome of molecular replacement and optimize molecular-replacement strategies.

Structural analysis of glycoproteins: building N-linked glycans with Coot

Newly improved tools for carbohydrate modelling in Coot are presented.

Effects of protein-crystal hydration and temperature on side-chain conformational heterogeneity in monoclinic lysozyme crystals

Measurement and modeling of the effects of dehydration and cryocooling on the conformational ensemble and solvent structure of monoclinic lysozyme crystals illuminate strong similarities in the local and global effects of these perturbations, which are attributed to their common effects on molecular packing within the crystal. These have an impact on the interpretation of differences between structures at T = 298 and 100 K and the choice of targets for variable-temperature crystallographic studies.

Gyre and gimble: a maximum-likelihood replacement for Patterson correlation refinement

Maximum-likelihood rigid-body refinement can be carried out to improve oriented models before the translation-function step of molecular replacement.

Exploiting distant homologues for phasing through the generation of compact fragments, local fold refinement and partial solution combination

ARCIMBOLDO_SHREDDER solves structures using fragments from low-homology models. Search fragments are improved through refinement or trimming against the experimental data. Consistent solutions are combined.

Structure and function of the type III pullulan hydrolase from Thermococcus kodakarensis

The type III pullulan hydrolase from Thermococcus kodakarensis (TK-PUL) possesses both pullulanase and α-amylase activities and has many potential applications in the industrial food-processing sector. Here, the crystal structure of TK-PUL is reported, which represents the first type III pullulan hydrolase structure to be solved, revealing N-terminal and C-terminal domains with significant differences from homologous structures.

The crystal structure of the lipo­aminopeptaibol helioferin, an antibiotic peptide from Mycogone rosea

The structure of the natural lipoaminopeptaibol helioferin is reported. It is a nonapeptide that contains only four proteinogenic amino-acid residues; two long aliphatic carbon chains protrude out from either side of the N-terminus of the helical peptide, giving rise to the corkscrew shape of the molecule.

Structures of the Mycobacterium tuberculosis GlpX protein (class II fructose-1,6-bis­phosphatase): implications for the active oligomeric state, catalytic mechanism and citrate inhibition

Structures of native and variants (T84S and T84A) of M. tuberculosis class II fructose-1,6-bisphosphatase are presented and compared with those of other homologs. The structure is a 222-symmetric homotetramer. Citrate was bound at a dimer interface and was found to be an inhibitor.

The crystal structure of the malic enzyme from Candidatus Phytoplasma reveals the minimal structural determinants for a malic enzyme

The crystal structure of the malic enzyme from aster yellows witches'-broom (Candidatus Phytoplasma) is reported. The structure showcases a minimal scaffold harbouring malic enzyme activity, shedding light on the evolution of complex malic enzymes.

Structural and functional roles of dynamically correlated residues in thymidylate kinase

Conformational changes upon ligand binding and the path for communication between the substrates and the protein are important in understanding the catalytic mechanism of thymidylate kinase.

The complex analysis of X-ray mesh scans for macromolecular crystallography

A method and software program, MeshBest, for the detection of individual crystals based on two-dimensional X-ray mesh scans are presented.

X-ray and UV radiation-damage-induced phasing using synchrotron serial crystallography

Multi-crystal serial crystallography data can be used for UV and X-ray radiation-damage-induced phasing.

The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum

The article by Isupov et al. [(2015). Acta Cryst. D71, 2344–2353] is corrected.

Hydrogen bonds are a primary driving force for de novo protein folding. Corrigendum

The paper by Lee et al. [(2017). Acta Cryst. D73, 955–969] is withdrawn.

Iron–Sulfur Clusters in Chemistry and Biology. Volume 2: Biochemistry, Biosynthesis and Human Diseases