Screening of Conditions that Facilitate Crystallization of Oligopeptidase B from Serratia Proteamaculans by Differential Scanning Fluorimetry

Crystallography Reports - Oligopeptidases B (OpdBs) are two-domain serine peptidases with trypsin-like substrate specificity belonging to the prolyl oligopeptidase family. These enzymes are...     

Crystallographic Study of Mutants and Complexes of Oligopeptidase B from Serratia proteamaculans

Crystallography Reports - The results of the structural studies of bacterial oligopeptidase B (OpB) belonging to the least well-studied prolyl oligopeptidase family are described. The screening of...     

Three-Dimensional Structure of a Mutant of Carboxypeptidase T from Thermoactinomyces vulgaris Bearing an Implanted S1' Subsite of Pancreatic Carboxypeptidase B Complexed with a Product Analog

Crystallography Reports - A mutant of bacterial carboxypeptidase T from Thermoactinomyces vulgaris (CPT5) with amino-acid substitutions in the S1' specificity pocket of the active site for the...     

Preparation of the recombinant НU-proteins from <Emphasis Type="Italic">S. melliferum</Emphasis> and <Emphasis Type="Italic">M. gallisepticum</Emphasis> and of their complexes with DS-DNA for structural NMR experiments

We created a high-performance system for expression of ¹³C, ¹⁵N-double-labeled recombinant НU-proteins from mycoplasms S. melliferum (HUSpm) and M. gallisepticum (HUMgal), and a purification protocol that yields protein samples suitable for structure studies by high-resolution NMR. Using these proteins we optimized the conditions of NMR experiments and obtained two-dimensional heteronuclear ¹H/¹⁵N-HSQC and ¹H/¹³С-HSQC-CT NMR spectra of free НU-proteins (HUSpm and HUMGal), and 1H/15N-HSQC spectrum of a complex between HUSpm and a double-stranded DNA (ds-DNA). The techniques we created are applicable in the studies of НU-proteins from other organisms. They allow analyzing structure and dynamics of free proteins and of their conformational changes induced by binding of various ds-DNAs or of DNA binding inhibitors.     

Erratum to: Preliminary X-ray Diffraction Analysis of the Envelope (E) Protein of Far-Eastern Tick-Borne Encephalitis Virus Subtype (Sofjin Strain)

Crystallography Reports - An Erratum to this paper has been published: https://doi.org/10.1134/S1063774522070501