09 angstrom by direct methods. The protein chain, which encompasses the first 104 residues of the full 220-residue selleck chem Pazopanib protein, adopts the characteristic oligonucleotide/oligosaccharide-binding (OB) structure consisting of a five-stranded beta-barrel filled with hydrophobic residues and equipped with four loops extending from the barrel. In the crystal two protomers dimerize, forming a six-stranded antiparallel beta-sheet. The structure of the N-terminal OB domain of T. tengcongensis shows significant differences compared with mesophile PriBs. While in all other known structures of PriB a dimer is formed by two identical OB domains in separate chains, TtePriB contains two consecutive OB domains in one chain.
However, sequence comparison of both the N-terminal Inhibitors,Modulators,Libraries and the C-terminal domains of TtePriB suggests that they have analogous structures and that the natural protein possesses a structure similar to a dimer of two N-terminal domains.
A new application of the ScrewFit algorithm [Kneller & Calligari (2006), Acta Cryst. D62, 302-311] is presented which adds the detection of protein secondary-structure elements to their detailed geometrical description in terms of a curve with intrinsic torsion. The extension is based on confidence and persistence criteria for the ScrewFit parameters which are established by analyzing the structural fluctuations of standard motifs in the SCOP fold Inhibitors,Modulators,Libraries classes. Inhibitors,Modulators,Libraries The agreement with the widely used DSSP method is comparable with the general consensus among other methods in the literature. This combination of secondary-structure detection and analysis is illustrated for the enzyme adenylate kinase.
Methods have previously been developed to measure detergent concentration in membrane-protein samples, but most have significant limitations, Inhibitors,Modulators,Libraries Cilengitide such as requiring specialized equipment or consuming a significant amount of precious sample. This work explores the use of 2,6-dimethylphenol in a phenol-sulfuric acid assay to accurately measure the concentration of common glycosidic-based detergents used in crystallization. This method is amenable to routine laboratory use, provides excellent sensitivity and significantly reduces the sample volume required. Using an Escherichia coli tyrosine kinase (Etk) construct as an example, it is shown that the crystallization potential of Etk is directly influenced by measurable changes in detergent concentration.
When embarking upon X-ray diffraction data collection from a potentially novel macromolecular crystal form, it can be useful to ascertain whether the measured data reflect a crystal form that is already recorded in the Protein Data Bank and, if so, whether it is part http://www.selleckchem.com/products/ganetespib-sta-9090.html of a large family of related structures.