Figure 1
Crystal screen results of proteins in standard and optimized buffers in two crystal screens: Index (Hampton Research) and P/PA (Table 3 ). Images were obtained using a Rhombix automated imager using either bright field or polarized light. The wells are presented in pairs: the left image is of standard buffer and the right image is of optimized buffer. (a) Two examples of catalase are shown. The left pair is Index No. 91 and the right pair is P/PA No. 39. Here, the optimal buffer showed only precipitate. (b) Examples of thaumatin crystals grown from sodium/potassium tartrate are shown. The left pair is from Index No. 31 and the right pair is from P/PA No. 21. Large single crystals grew in optimized buffer and only a light oily precipitate formed in the standard buffer. (c) Positive results for xylanase are presented for both standard and optimal buffer. The visual quality of the crystals was far superior in the optimal buffer. The left pair is Index No. 75 and the right pair is P/PA No. 27. (d) The α-lactalbumin crystals showed comparable results in both standard and optimized buffer. The left pair is Index No. 2 and the right pair is P/PA No. 6. A modest improvement in solubility between buffers for α-lactalbumin did not translate into a dramatic improvement in crystal quality. (e) Examples of D-xylose isomerase crystals where large single crystals grew in optimized buffer with oily precipitate present in the standard buffer for many conditions. The left pair is Index No. 94 and the right pair is P/PA No. 65. |