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The crystal structure of the β-CD atenolol (1:1) inclusion compound has been solved from synchrotron powder diffraction data using direct-space search techniques.
Two novel complexes of calcium croconate Ca μ3-C5O5)(H2O)3 (I) and calcium oxalato-croconate Ca2 μ4-C5O5 Ca2 μ4-C5O52O) (II) have been synthesized by soft chemical routes and their crystal structures have been solved from single-crystal data.
Moreover, most structures of transmembrane proteins have been solved for proteins from bacteria and archae, and only a few have been solved from eukaryotic systems [1].
The structure of the RING-H2 domain has only been solved from residue 127 to 189, and so coordinates of Ala 190 were not available due to a flexible linker region between the RING-H2 domain and the C-terminal domain.
At present, all membrane protein X-ray structures have been solved from 3D crystals (type I or II) only.
Crystal structures of the globular HN receptor-binding β-propeller have been solved from three viral species: NDV (an Avulavirus) [ 10, 11], PIV5 (a Rubulavirus) [ 12] and PIV3 (a Respirovirus) [ 13].
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