4RI0
Serine Protease HtrA3, mutationally inactivated
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-12-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 118.981, 118.981, 167.860 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.758 - 3.272 |
| R-factor | 0.201 |
| Rwork | 0.199 |
| R-free | 0.23270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nzi |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.829 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.760 | 50.000 | 3.330 |
| High resolution limit [Å] | 3.270 | 8.860 | 3.270 |
| Rmerge | 0.085 | 0.028 | 0.855 |
| Number of reflections | 18953 | ||
| <I/σ(I)> | 8.7 | 2.72 | |
| Completeness [%] | 98.4 | 92.5 | 99.8 |
| Redundancy | 9.6 | 8.7 | 9.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 289 | 1 M potassium/sodium phosphate buffer, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
