forthcoming articles

The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section D: Structural Biology.

See also Forthcoming articles in all IUCr journals.

Accepted 23 July 2018

Identification of the site of oxidase substrate binding in the Scytalidium thermophilum catalase

The structure of S. thermophilum catalase in complex with its well known inhibitor 3-amino-1,2,4-triazole (3TR) revealed that the inhibitor occupies a surface pocket at the end of the lateral channel. This pocket corresponds to the site of NADPH binding in mammalian catalases. Peroxide independent phenolic substrate oxidation is likely to occur in a similar manner to NADPH oxidation.

Accepted 18 July 2018

Co-crystallization of human inositol monophosphatase with the lithium mimetic L-690,330

Crystal structure of human inositol monophosphatase in complex with the substrate-based inhibitor L-690,330 is reported.

Accepted 16 July 2018

Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography

We have determined multiple dose-dependent room temperature structures of copper nitrite reductase from microcrystals in a single silicon nitride fixed target chip. We describe separation of crystal polymorphs into distinct structures, together with characterization of X-ray irradiation effects through the dose series.

Accepted 13 July 2018

Precipitant–ligand exchange technique reveals ADP-binding mode in Mycobacterium tuberculosis de­thiobiotin synthetase

A crystallographic technique was developed to exchange protein-bound precipitants with ligands that competitively bind to the same site. This revealed unexpected binding modes for ADP in complex with M. tuberculosis dethiobiotin synthetase, an antituberculosis drug target.

Accepted 10 July 2018

Rational modification of vanillin derivatives to stereospecifically destabilize sickle hemoglobin polymer formation

Accepted 9 July 2018

Crystallographically correct but confusing presentation of structural models deposited in the Protein Data Bank

Attention is brought to the fact that many coordinate sets deposited in the Protein Data Bank are located outside of the unit cells and are sometimes presented in space groups with symmetry lower than the true space group, and that symmetric oligomers are sometimes scattered, making it harder for the users to interpret quaternary structures.

Accepted 9 July 2018

Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae

The symbionts of marine shipworms provide a rich reservoir of potential carbohydrate-active enzymes. Here, the 1.5 Å resolution three-dimensional structure of a T. turnerae GH8 xylanase is revealed and its potential in biomass degradation is highlighted.

Accepted 3 July 2018

The crystal structure of an essential high-temperature requirement protein HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique features

High-temperature requirement A (HtrA) proteins belong to the serine protease family and possess protease and PDZ domains. HtrA1 is an essential membrane protein in M. tuberculosis.

Accepted 1 July 2018

Lipid composition in fungal membrane models: effect of lipid fluidity

This article reports the fabrication and characterisation of simple lipid bilayer models of fungal membranes to allow the study of their dynamics and interactions under modelled in vivo conditions.

Accepted 29 June 2018

High-pressure protein crystal structure analysis of Escherichia coli di­hydrofolate reductase complexed with folate and NADP+

High-pressure crystal structure analysis of E. coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ was performed up to 800 MPa. A pressure-induced phase transition of monoclinic ecDHFR crystals and structural changes closely related to its reaction mechanism were observed.

Accepted 27 June 2018

New tools for the analysis and validation of cryo-EM maps and atomic models

Accepted 25 June 2018

Improving signal strength in serial crystallography with DIALS geometry refinement

For XFEL data, simultaneous refinement of multi-panel detector geometry with thousands of crystal models in the program DIALS improves the integrated signal quality and helps to reduce non-isomorphism

Accepted 25 June 2018

Structure and function of L-threonine-3-de­hydrogenase from the parasitic protozoan Trypanosoma brucei revealed by X-ray crystallography and geometric simulations

Relationships between the structure and function of a putative drug target for human African trypanosomiasis have been elucidated using X-ray crystallography and geometric simulations. The data presented provide insights into ligand binding and catalysis, giving direction to future rational drug design.

Accepted 20 June 2018

Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33

The X-ray crystal structure of Omp33 is reported at a resolution of 2.1 Å. The structure helps in understanding how A. baumannii outer membrane proteins contribute to the low permeability of the cell envelope and suggests that Omp33 may function as a ligand-gated channel.

Accepted 15 June 2018

The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order

Cryosolution thermal contraction is found to impact cryocooled protein and unit-cell volumes and conformations. In some cases, its adjustment can produce higher quality diffraction data.

Accepted 5 June 2018

Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

The complete post-fusion core structure of the Human coronavirus 229E spike protein was determined at 1.86 Å resolution. Comparison of the interactions between heptad repeats HR1 and HR2 in different human coronaviruses reveals some differences, which should be taken into consideration when designing pan-coronavirus HR2-mimicking inhibitors that target HR1.

Accepted 14 May 2018

Introducing SEC–SANS for studies of complex self-organized biological systems

Small-angle neutron scattering is coupled with on-line size exclusion chromatography. The obtained SEC-SANS is combined with SEC-SAXS and utilized to investigate solution structures of phospholipid nanodiscs with and without membrane proteins incorporated.

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