6DR3
Crystal structure of E. coli LpoA amino terminal domain
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] | 140 |
Detector technology | PIXEL |
Collection date | 2017-08-02 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.97717 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 70.001, 70.001, 97.802 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.697 - 2.101 |
R-factor | 0.1808 |
Rwork | 0.177 |
R-free | 0.21320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4p29 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.441 |
Data reduction software | DENZO (2.3.10) |
Data scaling software | HKL-2000 (2.3.10) |
Phasing software | PHASER (2.7.2) |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
Rmerge | 0.104 | 0.044 | 0.760 |
Rmeas | 0.109 | 0.046 | 0.837 |
Rpim | 0.032 | 0.013 | 0.339 |
Total number of observations | 160798 | ||
Number of reflections | 14791 | 1616 | 1451 |
<I/σ(I)> | 6.7 | ||
Completeness [%] | 99.8 | 99 | 99.6 |
Redundancy | 10.9 | 11.5 | 5.7 |
CC(1/2) | 0.999 | 0.692 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | Drops contained 0.5 ul protein and 0.5 ul precipitant and equilibrated against precipitant by vapor diffusion. Protein: 19 mg/ml in 50 mM NaCl, 1 mM dithiothreitol, 50 mM TrisHCl pH 7.5. Precipitant contained: 0.03 M magnesium chloride hexahydrate, 0.03 M calcium chloride dihydrate, 5% glycerol, 0.1 M Buffer System 1, pH 6.5, 10% PEG 20,000, 17% PEG 550 MME Buffer System 1: 30 mL MES (pH 3.11) was titrated with 24.1 mL Imidazole (pH 10.23) to a final pH of 6.5 |