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Protein crystallization using room temperature ionic liquids
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DOI：10.1021/cg060696t.png)
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摘要
En 中文
The ionic liquids (ILs) 1-butyl-3-methylimidizolium chloride ([C(4)mim]Cl), 1-butyl-3-methylimidizolium 2(2-methoxyethoxy)ethylsulfate ([C(4)mim][MDEGSO4]), and 1-butyl-1-methylpyrollidinium dihydrogenphosphate ([p1,4][DHP]) were tested for their effects on the crystallization of the proteins canavalin, beta-lactoglobulin B, xylanase, and glucose isomerase, using a standard high throughput screen. The crystallization experiments were set up with the ILs added to the protein solutions at 0.2 and 0.4 M final concentrations. Crystallization droplets were set up at three protein/precipitant ratios (1:1, 2:1, and 4:1), which served to progressively dilute the effects of the screen components while increasing the equilibrium protein and IL concentrations. Crystals were obtained for all four proteins at a number of conditions where they were not obtained from IL-free control experiments. Over half of the protein-IL combinations tested had more successful outcomes than negative outcomes, where the IL-free crystallization was better than the corresponding IL-containing outcome, relative to the control. One of the most common causes of a negative outcome was solubilization of the protein by the IL, resulting in a clear drop. In one instance, we were able to use the IL-induced solubilizing to obtain beta-lactoglobulin B crystals from conditions that gave precipitated protein in the absence of IL. The results suggest that it may be feasible to develop ILs specifically for the task of macromolecule crystallization.
Keyword:
STABILITY
BIOCATALYSIS
CANAVALIN
SOLVENTS
SALTS
期刊
C
IF:
3.4
论文数:
1.6W
被引数:
3.5W
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