5CP0
MAS complex structure of peptide deformylase from Xanthomonas oryzae pv oryzae
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 4A |
| Synchrotron site | PAL/PLS |
| Beamline | 4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-20 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.99 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 58.736, 58.736, 265.360 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.370 - 2.000 |
| R-factor | 0.18226 |
| Rwork | 0.180 |
| R-free | 0.21660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3DLD |
| RMSD bond length | 0.026 |
| RMSD bond angle | 2.337 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | HKL-2000 |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.652 | |
| Number of reflections | 20724 | |
| <I/σ(I)> | 36.2 | 4.6 |
| Completeness [%] | 98.6 | 95.7 |
| Redundancy | 9.9 | 9.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 287 | 0.05M Cadmium sulfate, 0.1M HEPES, 2.0M Sodium acetate trihydrate, pH 7.5 |
