November 2018 issue
Highlighting the structure-based approach to combatting sickle cell disease taken by Safo and coworkers.
In this article, the status of the STARGazer data-processing software and its data-processing algorithms are described in detail. The STARGazer data-processing software is used for neutron time-of-flight single-crystal diffraction data collected using the IBARAKI Biological Crystal Diffractometer.
The crystal structures of two fimbrial adhesins from the uropathogen P. mirabilis are reported as a first step towards unveiling their role in pathogenesis. Despite lacking significant sequence homology, the two structures are very similar.
Quantum-mechanics/molecular-mechanics (ONIOM) X-ray macromolecular refinement using the program DivCon integrated with PHENIX is reported.
The crystal structure of α-L-rhamnosidase, a biotechnologically important enzyme isolated from Aspergillus terreus, reveals its active-site architecture, domain organization and native glycosylation.
It is demonstrated that using three-dimensional profile fitting of Bragg peaks increases the accuracy and resolution of neutron crystallographic data collected from proteins and reveals new features in nuclear density maps calculated from these data.
A detailed analysis of a winged helix–turn–helix family transcriptional regulator that positively regulates archaeal biofilm formation is reported.
Crystal structures of Klebsiella pneumoniae pullulanase (KPP) in complex with α-, β- or γ-cyclodextrin were determined at around 1.98–2.59 Å resolution. The cyclodextrins interact with CBM41 and the active site of KPP. In the active site, Phe746 interacts with the inner cavity of the cyclodextrin rings. The strong inhibition of KPP by β-cyclodextrin is caused by the optimized interaction between β-cyclodextrin and the side chain of Phe746. These structures and the kinetic parameters of recombinant pullulanase and its F746A variant revealed the importance of Phe746 in the selective binding of cyclodextrins.