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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



 



In situ proteolysis of N-terminal His tag with thrombin improved diffraction quality of AKR1C3 crystals
In situ specific proteolytic removal of His-tag by thrombin improves the morphology and diffraction quality of crystals of human aldo-keto reductase 1 C3.



Expression, purification and X-ray crystallographic characterization of CD163 long-range scavenger receptor cysteine-rich repeat
CD163 long-range scavenger receptor cysteine-rich (SRCR) repeat was prepared in Drosophila system and crystallized under the condition of 20% PEG 4000, 0.15 M potassium sodium tartrate tetrahydrate pH8.5. X-ray crystallographic characterization of this long-range SRCR repeat will provide the structural and functional information for the scavenger receptor (SR) superfamily.



Crystal structure of highly glycosylated human leukocyte elastase in complex with an S2′-site binding inhibitor
A novel binding mode of a small-molecule inhibitor of human leukocyte elastase is revealed by its co-crystal structure with the enzyme. In the structure, a comparatively large part of the N-glycan chains attached to the enzyme is visible.



Improved protein crystal identification by using 2,2,2-trichloroethanol as a fluorescence enhancer
Protein crystal labelling with 2,2,2-trichloroethanol for a more sensitive detection with UV light is described.



Crystal structures of human CK2α2 in new crystal forms arising from a subtle difference in salt concentration
New crystal forms of human CK2α2 were discovered and one showed improved crystallographic resolution to a maximum of 1.89 Å.



The putative siderophore-interacting protein from Vibrio anguillarum: protein production, analysis, crystallization and X-ray crystallographic studies
Siderophore-interacting proteins (SIPs) can reduce ferric iron to ferrous iron and cause iron to be released from the ferric siderophore complex. The SIP from V. anguillarum 775 has been expressed, purified and crystallized. The crystal diffracted to 1.113 Å resolution, which is the highest resolution so far observed for a member of the SIP family.



Crystal structure of chorismate mutase from Burkholderia thailandensis
The recombinant production and crystal structure of chorismate mutase from B. thailandensis are presented.






Crystal structure of the mouse innate immunity factor bacterial permeability-increasing family member A1
The crystal structure of mouse BPIFA1 was solved at 2.5 Å resolution and compared with those of structural homologs.



A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase
Trehalose is used in the cryoprotection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) crystals and induces conformational changes in GAPDH from E. coli. The conformational changes were independent of the duration of cryoprotectant soaking for up to 10 min.



Making glycoproteins a little bit sweeter with PDB_REDO
The results and challenges of carbohydrate handling in the current PDB_REDO databank are discussed.



Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution
The three-dimensional structure of a fungal arabinofuranosidase from CAZY family GH62 has been solved at 1.25 Å resolution in complex with the bespoke arabinofuranosidase inhibitor AraDNJ, shedding light on the activity of this catalyst in the enzymatic deconstruction of arabinoxylans.