Tables for
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 25.2, p. 696

Section Relative Wilson scaling

W. Fureya* Relative Wilson scaling

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With this method, the derivative scattering, on average, is made equal to the native scattering by plotting [-\ln \left({\langle F_{PH}^{2}\rangle \over \langle F_{P}^{2}\rangle}\right) \ versus \ \left\langle {\sin^{2} (\theta) \over \lambda^{2}}\right\rangle, \eqno(] with the averages taken in corresponding resolution shells. A least-squares fit of a straight line to the plot yields a slope equal to [2(B_{PH}-B_{P})] (twice the difference between overall isotropic temperature parameters for derivative and native data sets) and an intercept of ln [K^{2}]. From these values, the derivative data are put on the scale of the native by multiplying each derivative amplitude by [K \exp \left[(B_{PH} - B_{P}) {\sin^{2} (\theta) \over \lambda^{2}}\right]. \eqno(]

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