3SO3
Structures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-09-08 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 64 |
| Unit cell lengths | 130.598, 130.598, 96.941 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.880 - 2.100 |
| R-factor | 0.162 |
| Rwork | 0.161 |
| R-free | 0.19400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eax |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.637 |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 113.000 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.087 | 0.863 |
| Number of reflections | 54872 | |
| <I/σ(I)> | 11.7 | 2.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.3 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 16% PEG 3350, 0.23 M MgSO4, 0.4% isopropanol, 3% glycerol, 0.12 M AMSO4, vapor diffusion, hanging drop, temperature 293k, VAPOR DIFFUSION, HANGING DROP |
