Structural characterization and biochemical analysis of ID2, an inhibitor of DNA binding 4

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Structural characterization and biochemical analysis of ID2, an inhibitor of DNA binding 4

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Figure 10: HLH24-82-L crystals in 0.1 M MES pH 6.5, 2.5 M Lithium Acetate grown at 18°C (A) crystals crushed and used as stock for microseeding (B) 1:10 dilution of seed stock (C) 1:100 dilution of seed stock (D) 1:1000 dilution of seed stock Since there were numerous HLH-containing proteins in the PDB but none from the ID family, the closest homologous structure from the PDB was chosen for use in molecular replacement studies. Because ID2 was completed before ID3 was deposited in the PDB, the closest homologues structure, NeuroD1, had only a 30% identity. Hence, to prepare for the possibility that the template models were not suitable for molecular replacement, a seleno-methionine replaced HLH24-82-L was made (HLH24-82-L-Se-Met). The same screens were used to test for crystal growth ! 41! . ! 41 ! Figure 10: HLH 24- 82-L crystals in 0.1 M MES pH 6.5, 2.5 M Lithium Acetate grown at 18°C (A) crystals crushed and used as stock for microseeding (B) 1:10 dilution of seed stock. stock for microseeding (B) 1:10 dilution of seed stock (C) 1:100 dilution of seed stock (D) 1:1000 dilution of seed stock Since there were numerous HLH-containing proteins in the PDB. models were not suitable for molecular replacement, a seleno-methionine replaced HLH 24- 82-L was made (HLH 24- 82-L-Se-Met). The same screens were used to test for crystal growth

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