5HMA
Crystal structure of MamO protease domain from Magnetospirillum magneticum (Ni bound form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.116 |
| Spacegroup name | P 4 3 2 |
| Unit cell lengths | 129.163, 129.163, 129.163 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.666 - 2.299 |
| R-factor | 0.1852 |
| Rwork | 0.184 |
| R-free | 0.20870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5MH9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.090 |
| Data reduction software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
| Rmerge | 0.085 | 0.037 | 0.897 |
| Rmeas | 0.089 | 0.039 | 0.933 |
| Rpim | 0.025 | 0.011 | 0.256 |
| Total number of observations | 214349 | ||
| Number of reflections | 16999 | ||
| <I/σ(I)> | 12.3 | ||
| Completeness [%] | 99.9 | 99.3 | 100 |
| Redundancy | 12.6 | 11.2 | 13.1 |
| CC(1/2) | 0.999 | 0.858 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 291 | 50mM Na Acetate pH 4.6, 3.6M NH4Cl, 5% glycerol |






