3H09
The structure of Haemophilus influenzae IgA1 protease
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-05-12 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.86 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 94.385, 131.872, 111.813 |
| Unit cell angles | 90.00, 113.11, 90.00 |
Refinement procedure
| Resolution | 33.180 - 1.750 |
| R-factor | 0.162 |
| Rwork | 0.161 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1wxr |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.430 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (1.3.3) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.115 | 0.043 | 0.749 |
| Number of reflections | 251843 | ||
| <I/σ(I)> | 16.688 | ||
| Completeness [%] | 99.9 | 99.9 | 99 |
| Redundancy | 7.4 | 7.7 | 5.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | 10% PEG 20,000, 0.1M Sodium acetate pH 5.0, 0.1M dihydrogen phosphate, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
