PubMed · 9438862
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G J Kleywegt, R J Read. 1997-12-15. Not your average density.. https://doi.org/10.1016/s0969-2126(97)00305-5
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Three different methods are currently used for the study of high-resolution structures of membrane proteins: X-ray crystallography, electron crystallography, and nuclear magnetic resonance (NMR) spectroscopy. Thus far, all methods combined have yielded a rather modest number of crystal structures that have been solved at the atomic level. It is hypothesized here that different methods may select different populations of proteins on the basis of various properties. Thus, protein stability may be a significant factor in the formation of three-dimensional (3D) crystals from detergent solutions, since exposure of hydrophobic protein zones to water may cause structural perturbation or denaturation in conformationally labile proteins. This is different in the formation of two-dimensional (2D) crystals where a protein remains protected in its native membrane environment. A biological selection mechanism may therefore be operative in that highly ordered lattices may form only if strong protein-protein interactions are relevant in vivo, thereby limiting the number of proteins that are amenable to electron crystallography. Keeping a protein in a bilayer environment throughout 3D crystallization maintains the lateral pressure existing in native membranes. This can be accomplished by using lipidic cubic phases. Alternatively, the hydrophobic interface of a membrane protein may be spared from contact with water by crystallization from organic solvents where the polar caps are protected in reverse micelles by using appropriate detergents. Some of the criteria that are useful in optimizing the various approaches are given. While the usefulness of complementary methods seems obvious, the results presented may be particularly critical in recognizing key problems in other structural approaches.
The process for the synthesis of flyash-based zeolites (FAZs) are presented, which basically includes alkaline treatment of flyash by a fusion method, followed by hydrothermal crystallization. Zeolite-Y has been identified, and conditions have been optimized for their synthesis by the fusion method. Optimal conditions for synthesis of Zeolite-Y are a NaOH/flyash ratio of 1.2:1, fusion temperature between 500 degrees C and 600 degrees C, crystallization time of 8-10 h and crystallization temperature between 100 degrees C and 110 degrees C. The cation exchange capacity (CEC) of FAZ-Y ranges between 400 and 450 meq/100 g. The surface area of FAZs (500-600 m(2)/g) compare well with the commercial zeolites procured from Mobil Oil. Morphological characterization of FAZ using scanning electron microscopy (SEM) reveals cubic structure, and XRD data reveal unit cells to be cubic system.
Scores calculated from intermolecular contacts of proteins in the crystalline state are used to differentiate monomeric and homodimeric proteins, by classification into two categories separated by a cut-off score value. The generalized classification error is estimated by using bootstrap re-sampling on a nonredundant set of 172 water-soluble proteins whose prevalent quaternary state in solution is known to be either monomeric or homodimeric. A statistical potential, based on atom-pair frequencies across interfaces observed with homodimers, is found to yield an error rate of 12.5%. This indicates a small but significant improvement over the measure of solvent accessible surface area buried in the contact interface, which achieves an error rate of 15.4%. A further modification of the latter parameter relating the two most extensive contacts of the crystal results in an even lower error rate of 11.1%.