3NJG
K98A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis.
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 | 99.901, 99.901, 100.589 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 32.800 - 1.920 |
| R-factor | 0.1696 |
| Rwork | 0.168 |
| R-free | 0.19580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n55 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.528 |
| 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] | 32.800 | 40.000 | 1.980 |
| High resolution limit [Å] | 1.920 | 4.390 | 1.920 |
| Rmerge | 0.182 | 0.117 | 0.633 |
| Number of reflections | 14934 | ||
| <I/σ(I)> | 5.8 | 2.51 | |
| Completeness [%] | 100.0 | 99.8 | 99.9 |
| Redundancy | 8.7 | 8.9 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 291 | 2.5 M sodium chloride, 0.1 M acetate buffer, 0.2 M lithium sulfate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
