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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



 



Structure of the mouse acidic amino-acid decarboxylase GADL1
The structure of the mouse glutamic acid decarboxylase-like protein 1 (GADL1) is described. The structure gives new insights into the function of GADL1 and related decarboxylases.






Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis
The cloning, purification, biophysical characterization, crystallization and X-ray diffraction analysis of the two periplasmic domains of N. meningitidis DsbD, a disulfide reductase essential for the viability of this human pathogen, are reported.






Structure and stability of the Human respiratory syncytial virus M2–1 RNA-binding core domain reveals a compact and cooperative folding unit
A high-resolution crystal structure of the M2–1 RNA-binding domain of Human syncytial respiratory virus was determined. A combination of crystallography and SAXS indicated its role in C-terminal extension.



Structure of aspartate β-semialdehyde dehydrogenase from Francisella tularensis
The crystal structure of aspartate β-semialdehyde dehydrogenase from F. tularensis has been determined.



Crystal structure of cytoplasmic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae
Structural comparison of the apo structure of S. cerevisiae thiolase with the structure of the CoA-bound complex of human mitochondrial acetoacetyl-CoA thiolase raises the alternate hypothesis that its identical ordered conformation is induced by substrate binding.



The novel thermostable cellulose-degrading enzyme DtCel5H from Dictyoglomus thermophilum: crystallization and X-ray crystallographic analysis
In this study, a new endo-β-(1,4)-glucanase isolated from the thermophilic D. thermophilum, denoted DtCel5H, has been identified, produced and crystallized. In addition, it is shown that this enzyme possesses cellulose-degradation activity and is highly thermostable. Structural investigations of this new cellulase will offer the opportunity to design and develop enzymes with optimal biotechnological applications.