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Forthcoming article in Acta Crystallographica Section F Structural Biology Communications



Acta Crystallographica Section F: Structural Biology Communications is a rapid all-electronic journal, which provides a home for short communications on the crystallization and structure of biological macromolecules. Structures determined through structur



 



Identification, biochemical characterization and crystallization of the central region of human ATG16L1
Structural information on the 607-amino-acid human ATG16L1 protein is restricted to the N-terminal ATG5-binding domain and the recently reported structure of the C-terminal WD40 domain, whereas structural information for the central region of ATG16L1 remains elusive. In this work, the identification, purification, biochemical characterization and crystallization of a stable ATG16L1 subfragment comprising residues 72–307, comprising the so far structurally uncharacterized central region of ATG16L1, are presented.



Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 Å
The highest resolution structure of bacterial type II NADH:quinone oxidoreductase was determined at 2.15 Å resolution. This structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules.



Crystal structure of the starch-binding domain of glucoamylase from Aspergillus niger
The crystal structure of the starch-binding domain of glucoamylase shows that the conformation of the region surrounding the disulfide bond is highly flexible.



Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP
The expression, large-scale crystallization and neutron diffraction analysis of the human HSP70 ATPase domain are reported.