1T7I
The structural and thermodynamic basis for the binding of TMC114, a next-generation HIV-1 protease inhibitor.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 210 |
Collection date | 2003-06-26 |
Wavelength(s) | 0.9 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.858, 58.040, 61.656 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.260 - 1.350 |
Rwork | 0.163 |
R-free | 0.20005 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f7a |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 43.000 |
High resolution limit [Å] | 1.350 |
Rmerge | 0.044 |
Number of reflections | 39998 |
<I/σ(I)> | 13.5 |
Completeness [%] | 98.0 |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 280 | AMMONIUM SULPHATE, SODIUM PHOSPHATE, SODIUM CITRATE, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 280K |