3MR1
Crystal structure of methionine aminopeptidase from Rickettsia prowazekii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.480, 114.850, 115.800 |
| Unit cell angles | 90.00, 92.66, 90.00 |
Refinement procedure
| Resolution | 42.400 - 2.000 |
| R-factor | 0.17271 |
| Rwork | 0.171 |
| R-free | 0.21229 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xnz |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.410 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.400 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.080 | 0.260 |
| Number of reflections | 73427 | |
| <I/σ(I)> | 15.32 | 4.6 |
| Completeness [%] | 98.1 | 84 |
| Redundancy | 4.91 | 3.63 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 0.1 M SPG buffer pH 8.0, 25% PEG 1500 with 20% ethylene glycol as cryoprotectant, 29 mg/mL protein, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
