3NJL
D116A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis, at pH7.5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-13 |
| Detector | SBC-3 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 100.151, 100.151, 100.216 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 31.200 - 1.750 |
| R-factor | 0.166 |
| Rwork | 0.166 |
| R-free | 0.17200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n55 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.602 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 31.200 | 1.800 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.043 | 0.786 |
| Number of reflections | 19469 | |
| <I/σ(I)> | 11.1 | 2.45 |
| Completeness [%] | 99.6 | 99.1 |
| Redundancy | 10.3 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 0.1 M HEPES buffer, 0.5 M magnesium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
