Crystal transfer experiments carried out with crystals of tryanosomal triosephosphate isomerase (TIM)
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The crystal structures of CDD-1, the intrinsic class D β-lactamase from the pathogenic Gram-positive bacterium Clostridioides difficile, and its complex with cefotaxime
2019, Journal of Structural BiologyCitation Excerpt :Crystal soaking experiments with substrates and inhibitors in the original crystallization buffer proved to be problematic due to the presence of a tightly bound sulfate anion in the active site. In order to remove the sulfate, crystals of apo-CDD-1* were transferred into a buffer comprising 0.1 M MES pH 5.6, 85% 2-methyl-2,4-pentandiol (MPD) following established methods (Schreuder et al., 1988; Wierenga et al., 1992). Briefly, 10 μL droplets of the original crystallization buffer were suspended over a series of reservoirs containing increasing concentrations of alternate precipitants.
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