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 |