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Efficacy of the Solvent Model

Table iii shows the solvent and scaling parameters for three structures. It shows that the addition of a solvent model can lower the R value of a refined structure by up to 2%.

Table iii also shows that the solvent parameters for these three structures are remarkably similar. This similarity is consistent with the notion that ``water is water''. It seems reasonable that solvent will be excluded in a similar fashion from all protein molecules, and because tex2html_wrap_inline635 describes the transition from solvent to protein it should be similar from one structure to another.

However not all mother liquors have the same electron density. tex2html_wrap_inline631 should vary from structure to structure. The structures in Table iii are listed in order of increasing solvent electron density. Thermolysin crystals are stored in water with 7% DMSO and little else. T4 lysozyme crystals are immersed in 2M phosphate buffer. Although mass density is not strictly proportional to electron density the electron density of T4 lysozyme mother liquor should be higher than that of thermolysin.

Because the structures were refined without the low-resolution data and without solvent models, there is a correction to the average temperature factor in both sets of scale factors for each structure. In each case the average temperature factor increases when the solvent model is added. An additional trend can be observed. The increase for the thermolysin inhibitor which was refined to 1.6Å resolution was 2.8Å tex2html_wrap_inline675 while the increase for the bacteriochlorophyll containing protein (refined to 1.9Å) was 6.0Å tex2html_wrap_inline675 . The lower the resolution of the data set, the more important is the contribution of the lowest resolution data.

It is true that the R value calculated with both low-resolution data and a solvent model will be higher than the R value for the same coordinate set calculated with the low-resolution data eliminated. As seen in Table iii the R value for the thermolysin:inhibitor complex using the 20 to 1.6Å data is 17.5%. When the inner resolution limit is set to 5.5Å the R value drops to 17.1%. Some investigators may consider the lower R value justification for rejecting these data. This is incorrect reasoning. In a statistical analysis, the model can never be used to assess the data. It is clear that the lower R value does not represent a better model -- The same model is used in both cases. The lower R value is simply an artifact of the method used in its calculation.


next up previous
Next: Acknowledgements Up: How to Model a Previous: Parameter Determination
Dale Edwin Tronrud

Thu Nov 20 13:34:16 PST 1997