Subscribe: Forthcoming article in Acta Crystallographica Section D: Biological Crystallography
Preview: Forthcoming article in Acta Crystallographica Section D: Biological Crystallography

Forthcoming article in Acta Crystallographica Section D Structural Biology

Acta Crystallographica Section D: Structural Biology welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports o


Combining X-ray and neutron crystallography with spectroscopy
The use of neutron crystallography and in situ spectroscopy to study enzyme mechanism is discussed.

On the interpretation of reflectivity data from lipid bilayers in terms of molecular-dynamics models
A method is presented for producing continuous scattering length density profiles from simulated MD structures of biomembranes, for analyzing reflectometry data from lipid layers.

Structure of the cyanobactin oxidase ThcOx from Cyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD
The first crystal structure of ThcOx, a cyanobactin oxidase, has been determined to 2.65 Å resolution using S-SAD phasing. This is the first structure reported from the purpose-designed long-wavelength beamline I23 at Diamond Light Source.

Perdeuteration, crystallization, data collection and comparison of five neutron diffraction data sets of complexes of human galectin-3C
Perdeuteration, purification and the growth of large crystals of the carbohydrate-recognition domain of galectin-3C are desribed. Five neutron diffraction data sets have been collected at four neutron sources; these are compared and two are merged.

A public database of macromolecular diffraction experiments
The Integrated Resource for Reproducibility in Macromolecular Crystallography (IRRMC) is a large, scalable and searchable web-accessible archive of protein crystallography diffraction experiments organized according to metadata.

Using more than 801 296 small-molecule crystal structures to aid in protein structure refinement and analysis
A guide to how the Cambridge Structural Database can be used to aid macromolecular crystallography.

Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum
The thermostable glucuronoxylan endo-β-1,4-xylanase from C. thermocellum cleaves the xylan chain specifically at sites containing 4-O-methylglucuronic acid substitutions. The structure of the ligand-bound enzyme mutant E225A solved at 1.17 Å resolution shows binding of the xylotetraose-cleavage oligosaccharides at subsites −3 to +2.

Glycoblocks: a schematic three-dimensional representation for glycans and their interactions
With structural glycoscience finally gaining popularity, the need for a clear way of depicting glycans and their interactions in three dimensions is more pressing than ever. Here the Glycoblocks representation is introduced, which combines a simplified bonding-network depiction with the familiar two-dimensional glycan notation brought into three-dimensions.