5UWA
Structure of E. coli phospholipid binding protein MlaC
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.116 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.630, 115.890, 133.220 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.718 - 1.501 |
| R-factor | 0.1387 |
| Rwork | 0.138 |
| R-free | 0.16750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | based on homology model with 2QGU as a template |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.202 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.500 |
| Number of reflections | 83295 |
| <I/σ(I)> | 22.2 |
| Completeness [%] | 98.5 |
| Redundancy | 7.2 |
| CC(1/2) | 0.570 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 0.1 M citric acid pH 3.5 and 1.6 M ammonium sulfate |






