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![[Figure 4]](gj5234fig4mag.jpg)
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Figure 4
Dialysis experiment with variation of the temperature in the case of growth of large crystals of the urate oxidase complex with 9-methyl uric acid. (a) Situation at the end of the third day. Once the concentration of the crystallization agent inside the dialysis button at T1 = 293 K has reached that of the reservoir solution, the formation of many small crystals of the Uox–9MUA complex is observed next to a few seeded crystals in the dialysis button. The temperature is increased to T2 = 298 K. (b) Situation after 10 min from dissolution of small crystals in excess at T2 = 298 K. Growth of a few crystals observed at T3 = 293 K during the first day (c) and 2 days after dissolution (d). (e) Growth of a few crystals and of one selected seeded crystal observed at T3 = 293 K 5 days after dissolution. Growth of the selected seeded crystal observed (f) 5 days, (g) 7 days and (h) 9 days at 293 K and (i) 12 days and (j) 17 days at T4 = 291 K after dissolution. (k) Schematic phase diagram (protein concentration versus temperature) incorporating some selected images (to be tracked in alphabetical order) to illustrate the optimization workflow in growing large Uox–9MUA complex crystals. In accordance with alternative workflow A2 (Section 2.3 ![[link]](../../../../../../logos/arrows/j_arr.gif) ), C1 represents the initial protein concentration used in the crystallization experiment (8 mg ml−1). C2 is weaker than the initial protein concentration, as it results from crystal growth in the metastable zone. C3 and C4 are then protein concentrations corresponding to the relative equilibrium points reached. |
![[Figure 4]](gj5234fig4.jpg)
 | JOURNAL OF APPLIED CRYSTALLOGRAPHY |
ISSN: 1600-5767
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