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A fast analytical method for calculating mask-based bulk-solvent scale factors and overall anisotropic correction factors is introduced.

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The crystal structures of the eubacterial translation initiation factor 2 in apo form and with bound GDP and GTP reveal conformational changes upon nucleotide binding and hydrolysis, notably of the catalytically important histidine in the switch II region.

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The notion of `resolution' is discussed and a formal definition applicable to various diffraction data sets, both complete and incomplete and both isotropic and anisotropic, is suggested.
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