 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](rf5022fig1mag.jpg)
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Figure 1
Protein production and crystallization. (a) SDS–PAGE analysis of the amidase elution fractions showing a trace amount of a contaminant which possibly contains EcDSCD. Fractions showing a purity of greater than 95% (120–300 mM imidazole) were pooled and further concentrated to 254 mg ml−1 as measured by the absorbance at 280 nm. The molecular weight of the His-tagged amidase is 47.3 kDa. The concentration of EcDSCD (the crystallized impurity) is roughly estimated as <0.1–0.2 mg ml−1 in a 10× concentrated amidase solution based on a band with a molecular weight of 26 kDa (we speculate that it is the band visible in the 30 mM imidazole elution lane). Red arrows show the approximate locations of the uncleaved and cleaved transferase based on molecular weights of 44 and 26 kDa, respectively. The image was analysed using ImageJ v.1.51j8 (https://imagej.nih.gov/ij/) to estimate the concentrations of total impurities and of EcDSCD. (b) A crystal of EcDSCD as mounted on a cryo-loop at the beamline. The crystal is roughly 35 × 35 × 30 µm in size. |
![[Figure 1]](rf5022fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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