3OCA
Crystal structure of peptide deformylase from Ehrlichia chaffeensis
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 | 2009-05-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9744 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 84.260, 64.430, 80.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.670 - 2.400 |
| R-factor | 0.195 |
| Rwork | 0.192 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n5n |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.283 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.069 | 0.487 |
| Number of reflections | 17678 | |
| <I/σ(I)> | 18.6 | 3.4 |
| Completeness [%] | 99.2 | 99.8 |
| Redundancy | 4.8 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 290 | 200MM AMMONIUM CITRATE, 20% PEG 3350; Protein at 28MG/ML, PH 8.5, VAPOR DIFFUSION, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
