 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](qh5028fig1mag.jpg)
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Figure 1
Oligomerization of NO66 is required for substrate binding and catalysis. (a) GST pull-down of NO66176–C by different fragments of Rpl8 fused to GST. Asterisks indicate the band corresponding to NO66176–C. (b) A comparison of the efficiency of wild-type NO66 and mutants. The products of the hydroxylation reaction were detected by LC-MS/MS and the data are semi-quantitative. (c, d) Comparison of the binding of wild-type NO66176–C (red) and mutant protein M2 (black) to GST-Rpl8193–C (c) and αKG (d). The ITC method was used to analyze the binding affinities. |
![[Figure 1]](qh5028fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
