3NJH
D37A 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 | 2006-04-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 3 |
| Unit cell lengths | 97.986, 97.986, 65.844 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 39.300 - 1.940 |
| R-factor | 0.1296 |
| Rwork | 0.127 |
| R-free | 0.15240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n55 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.677 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 39.300 | 50.000 | 1.970 |
| High resolution limit [Å] | 1.940 | 5.260 | 1.940 |
| Rmerge | 0.132 | 0.071 | 0.718 |
| Number of reflections | 51991 | ||
| <I/σ(I)> | 8.5 | 2.12 | |
| Completeness [%] | 100.0 | 99.5 | 100 |
| Redundancy | 5.5 | 5.7 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 0.2 M calcium chloride, 0.1 M Bis-Tris buffer, 45% 2-methyl-2,4-pentanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
