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By A. C. Zettlemoyer

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In the screening process therefore, the protein-laden mesophase is typically exposed to precipitant solutions 40 M. Caffrey that encompass hundreds, perhaps even thousands of different chemical compositions. , and all at different concentrations. Each component can potentially destabilize the mesophase. In a separate study using SAXS, we examined the compatibility of the default monoolein/water cubic phase with various commonly used precipitant screen solutions [13]. What we found was hardly surprising.

In one type of approach, it is sometimes possible to effectively correct the observed data and estimate what the observed intensities should have been in the absence of twinning; this is referred to as ‘detwinning’. In contrast, most approaches to structure determination and refinement take the reverse strategy, modeling the effects of twinning into the calculated intensities instead. O. Yeates As a precautionary note, it should be understood that the averaging effects of twinning tend to produce lower R-values for purely statistical reasons not reflective of model quality.

Experimental evidence in support of aspects of this model has been reported [9]. Experience built up over the years working with the in meso method suggests that the mesophase behaviour observed during the course of crystallization mimics that of the monoolein/water system [4]. The implication therefore is that the protein solution has minimal effect on the phase behaviour of the hosting lipidic mesophase into which the protein is reconstituted. That solution, along with the target protein, typically includes lipid, detergent, buffers, and salt at a minimum.

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Nucleation by A. C. Zettlemoyer

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