3M0O
Crystal Structure of the Lys265Met mutant of monomeric sarcosine oxidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.90 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 72.565, 69.617, 73.978 |
| Unit cell angles | 90.00, 93.91, 90.00 |
Refinement procedure
| Resolution | 30.120 - 1.600 |
| R-factor | 0.175 |
| Rwork | 0.173 |
| R-free | 0.20800 |
| Structure solution method | Direct refinement from wild type coordinates |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.371 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.4.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.640 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.066 | 0.431 |
| Number of reflections | 92866 | |
| <I/σ(I)> | 17.2 | 2.1 |
| Completeness [%] | 96.2 | 85 |
| Redundancy | 4.8 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7 | 298 | 1.7 M Na/K phosphate buffer, vapor diffusion, temperature 298K, VAPOR DIFFUSION |
