2OC1
Structure of the HCV NS3/4A Protease Inhibitor CVS4819
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 2 |
Unit cell lengths | 222.936, 222.936, 75.158 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.700 |
Rwork | 0.189 |
R-free | 0.25900 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 2o8m |
RMSD bond length | 0.008 |
RMSD bond angle | 1.790 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (98.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 19837 | |
<I/σ(I)> | 23.3 | 3.3 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 277 | The protein (NS3 complexed with KK-NS4a(21-39)-KK peptide) was at 12-15 mg/ml in 15 mM MES, pH 6.5 1 M NaCl 20 mM b-mercaptoethanol. Hanging Drops were formed by mixing 4:l protein solution with 4:l {0.75-1.0 M NaCl 0.1M Na/K phosphate 0.1 M Mes, pH 5.8-6.1 20 mM b -mercaptoethanol} The drop was equilibrated the drops over 1 ml {(1.25-1.50 M) NaCl - 0.1M Na/K phosphate 0.1 M Mes, pH 5.6-5.8, 20 mM b-mercaptoethanol} , VAPOR DIFFUSION, HANGING DROP, temperature 277K |