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The crystal structure of the DsbB-DsbA-ubiquinone ternary complex has revealed a mechanism of protein disulfide bond generation in Escherichia coli.


A chromoprotein from Pleurotus salmoneostramineus has been purified and crystallized to give a needle-shaped crystal in space group C2. The crystal diffracts to 1.8 Å resolution with synchrotron radiation.



A general theoretical approach to the description of epitaxial layers with essentially different cell parameters and in-plane relaxation anisotropy is presented.