4E75
Structure of LpxD from Acinetobacter baumannii at 2.85A resolution (P21 form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-15 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.9794 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 106.679, 209.614, 107.633 |
| Unit cell angles | 90.00, 119.23, 90.00 |
Refinement procedure
| Resolution | 48.150 - 2.850 |
| R-factor | 0.23668 |
| Rwork | 0.234 |
| R-free | 0.27988 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pm0 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.444 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.940 |
| High resolution limit [Å] | 2.840 | 2.840 |
| Rmerge | 0.113 | 0.585 |
| Number of reflections | 94647 | |
| <I/σ(I)> | 8.7 | 1.8 |
| Completeness [%] | 99.5 | 99.5 |
| Redundancy | 2.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 2ul of 15mg/ml protein, 2ul of 24% PEG3350, 0.2M Ammonium formate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
