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• W2084501818 abstract "When the first three-dimensional structures of protein molecules were determined at atomic resolution, there remained a significant concern as to the conformational similarity between proteins in a crystalline lattice and those in aqueous solution. It is now widely accepted that the structure of a biological macromolecule in the crystal is virtually the same as its structure in solution. It is often equally important, however, to compare the reactivity of a protein in a crystalline environment with that in solution. Specifically, the investigator must often assess whether the crystal lattice imposes subtle structural differences, with respect to a fully active molecule in the cell, that could influence mechanism or reactivity. This is particularly important in the development of time-resolved crystallographic studies of biological intermediates in order to properly estimate the lifetime of a specific intermediate, and also in the light of the rapidly growing number of molecular and cellular biologists now making significant use of X-ray crystallographic studies and collaborations." @default.
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• W2084501818 date "1995-10-01" @default.
• W2084501818 modified "2023-10-03" @default.
• W2084501818 title "Direct measurement of reactivity in the protein crystal by steady-state kinetic studies" @default.
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• W2084501818 doi "https://doi.org/10.1016/s0969-2126(01)00235-0" @default.
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