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Molecular basis of agonism and antagonism in the oestrogen receptor
The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.
Can anomalous signal of sulfur become a tool for solving protein crystal structures?
Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.
Novel approach to phasing proteins: derivatization by short cryo-soaking with halides.
This approach has been tested successfully on four different proteins and has been used to solve the structure of a new protein of molecular weight 30 kDa.
High resolution structures of holo and apo formate dehydrogenase.
Three-dimensional crystal structures of holo (ternary complex enzyme-NAD-azide) and apo NAD-dependent dimeric formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 have
Protein crystallography for non‐crystallographers, or how to get the best (but not more) from published macromolecular structures
This review attempts to provide a brief outline of technical aspects of crystallography and to explain the meaning of some parameters that should be evaluated by users of macromolecular structures in order to interpret, but not over‐interpret, the information present in the coordinate files and in their description.
Triclinic lysozyme at 0.65 A resolution.
The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation, and the occupancies of the water sites were refined.
The Catalytic Domain of Escherichia coli Lon Protease Has a Unique Fold and a Ser-Lys Dyad in the Active Site*
Alignment of the P domain catalytic pocket with those of several Ser-Lys dyad peptide hydrolases provides a model of substrate binding, suggesting that polypeptides are oriented in the Lon active site to allow nucleophilic attack by the serine hydroxyl on the si-face of the peptide bond.
The DCX-domain tandems of doublecortin and doublecortin-like kinase
A solution structure of the N-terminal DCX domain of human doublecortin and the equivalent domain from human DCLK are reported, which show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains.