issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

September 2020 issue

Highlighted illustration

Cover illustration: Radiation damage in bromophenol blue molecules [Plaza-Garrido et al. (2020), Acta Cryst. D76, 844-855]. The Fo - Fc map shows large red blobs over the positions of the Br atoms because of the loss of these atoms from radiation damage during data collection. The right panel shows lysozyme crystals soaked at a low BPB concentration after data collection: the upper image is a crystal without irradiation and the lower image is a crystal irradiated twice at two different positions. Yellow lines appear at the irradiated positions.

scientific commentaries

link to html
A new approach to in situ experimental phasing introduced by Lawrence et al. (2020, Acta Cryst. D76, 790–801) will be helpful for the macromolecular crystallography community.


link to html
The web server performs an assignment of nucleic acid conformations and presents the results for the intuitive annotation, validation, modeling and refinement of nucleic acids.

link to html
This study shows the usefulness of integrating automated crystallographic model-building pipelines. We ran the four most used pipelines (ARP/wARP, Buccaneer, Phenix AutoBuild and SHELXE) alone and in pairwise combinations, and compared the structures that they produced based on structure completeness and Rfree.


link to html
Engrailed homeodomain (EHD) is a low-molecular-weight DNA-binding protein that can potentially act as a molecular tool to target desired DNA sites in cells. The crystal structure of tandemly connected EHDs with R53A mutations revealed that the mutation does not interfere with the important base-specific interactions of the wild-type protein; instead, it works to properly modulate the DNA-binding affinity, leading to precise recognition of the target site.

link to html
X-ray crystal structures were determined of the wild type and an inactive mutant of α-amylase from the earthworm Eisenia fetida. Structural analyses reveal the molecular properties that are responsible for catalytic activity at low temperatures and substrate recognition.

research papers

link to html
The low-resolution 3D structure of a plant nucleotide pyrophosphatase/phosphodiesterase (NPP) solved by small-angle X-ray scattering is reported. The general structural features of plant NPPs are inferred. Structural analogies with, and differences from, mammalian NPPs are discussed.

link to html
The crystal structure of an epoxide hydrolase from Streptomyces sp. CBMAI 2042 was determined and revealed the conserved overall fold found in other α/β-hydrolases, despite its unusual hexameric quaternary structure. Although its primary sequence is similar to that of a Mycobacterium tuberculosis epoxide hydrolase, its active-site architecture, and particularly its volume, closely resembles the human epoxide hydrolase.

link to html
The crystal structure of Fab4 bound to the epitope of the bacteriophage P22 large terminase subunit, together with a 1.15 Å resolution crystal structure of the unliganded Fab4, which is the highest resolution ever achieved for a Fab, elucidate the principles governing the recognition of this novel helical epitope.

link to html
The crystal structure of bacteriophage T4 Spackle as determined by sulfur SAD phasing reveals a monomeric protein with a helical bundle fold and a disc-like overall shape. Spackle has an intramolecular disulfide bond and a bipolar surface-charge distribution, which are consistent with its proposed role as a lysozyme inhibitor that functions in the Escherichia coli periplasm.

addenda and errata

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