4E6T
Structure of LpxA from Acinetobacter baumannii at 1.8A resolution (P212121 form)
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 | 2010-09-13 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 71.696, 104.490, 106.979 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.610 - 1.800 |
| R-factor | 0.1795 |
| Rwork | 0.178 |
| R-free | 0.21137 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qia |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.268 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.600 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.083 | 0.372 |
| Number of reflections | 72800 | |
| <I/σ(I)> | 12.1 | 3 |
| Completeness [%] | 97.2 | 86.4 |
| Redundancy | 5 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 2ul of 15mg/ml protein, 2ul of 0.2M Ammonium citrate tribasic, 20% PEG 3350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
