3NJI
S114A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis.
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 | 2008-03-12 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 99.833, 99.833, 99.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.200 - 1.800 |
| R-factor | 0.1674 |
| Rwork | 0.166 |
| R-free | 0.18890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n55 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.609 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.200 | 50.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
| Rmerge | 0.068 | 0.045 | 0.613 |
| Number of reflections | 17886 | ||
| <I/σ(I)> | 14.1 | 1.97 | |
| Completeness [%] | 99.6 | 99.4 | 94.2 |
| Redundancy | 9.7 | 10 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 1 M ammonium sulfate, 0.1 M Bis-Tris buffer, 1% PEG-3350, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
