4E79
Structure of LpxD from Acinetobacter baumannii at 2.66A resolution (P4322 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 43 2 2 |
| Unit cell lengths | 64.667, 64.667, 463.814 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.600 - 2.660 |
| R-factor | 0.23708 |
| Rwork | 0.234 |
| R-free | 0.29973 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4e75 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.352 |
| 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 | 2.760 |
| High resolution limit [Å] | 2.660 | 2.660 |
| Rmerge | 0.120 | 0.572 |
| Number of reflections | 29759 | |
| <I/σ(I)> | 16.9 | 4.2 |
| Completeness [%] | 99.2 | 100 |
| Redundancy | 9.1 | 9.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 2ul of 12mg/ml protein, 2ul of 19% PEG3350, 0.4M magnesium acetate, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
