forthcoming articles

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

See also Forthcoming articles in all IUCr journals.

Accepted 16 October 2018

Combining crystallogenesis methods to produce diffraction-quality crystals of a psychrophilic tRNA-maturation enzyme

Advanced crystallogenesis methods, including microseed matrix screening, crystallization optimization by counter-diffusion and crystal detection by trace fluorescent labeling, were used in combination to successfully produce various diffracting crystal forms of a CCA-adding enzyme from the psychrophilic bacterium Planococcus halocryophilus.

Accepted 15 October 2018

Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae DSM5389

In the first step of the biosynthesis of trehalose, glycosyltrehalose synthase from S. shibatae DSM5389 has an optimum catalytic cavity for the intramolecular transglycosylation mechanism which converts the glucosidic bond between the last two glucose residues of amylose from an α-1,4 bond to an α-1,1 bond.

Accepted 3 October 2018

On cross-correlations, averages and noise in electron microscopy

The influence of noise on cross-correlations is revisited. Equations are provided describing the influence of noise on the cross-correlations between single images and averaged images and between averaged images.

Accepted 15 September 2018

X-ray crystallographic analysis of the catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus overexpressed in Brevibacillus choshinensis

The catalytic domain of α-1,3-glucanase FH1 from P. glycanilyticus FH11, which may be of application in dental care and the development of fungal cell-wall lytic enzymes, was expressed and purified, and the protein was crystallized using the sitting-drop vapor-diffusion method. Diffraction data were collected to a resolution of 1.6 Å.

Accepted 13 September 2018

Structure of undecaprenyl pyrophosphate synthase from Acinetobacter baumannii

The inhibition of undecaprenyl pyrophosphate synthase (UPPS) may be an effective strategy in combating the multidrug-resistant pathogen A. baumannii. The structure of UPPS from A. baumannii reported here may provide a structural basis for inhibitor design.

Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds