1CL7
ANTI HIV1 PROTEASE FAB
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1995-03-01 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.400, 58.800, 143.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 3.000 |
Rwork | 0.183 |
R-free | 0.28000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fbi |
RMSD bond length | 0.012 |
RMSD bond angle | 28.390 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 3.160 |
High resolution limit [Å] | 3.000 | 3.050 |
Rmerge | 0.133 | 0.350 |
Total number of observations | 40751 * | |
Number of reflections | 7832 * | 763 * |
<I/σ(I)> | 15 | 4 |
Completeness [%] | 99.5 | 100 |
Redundancy | 5.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 18 * | drop consists of equal volume of protein and precipitant solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Fab | 4 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | precipitant |
3 | 1 | reservoir | PEG4000 | 20 (%) | precipitant |