1EQ7
CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1999-03-19 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | H 3 2 |
Unit cell lengths | 34.363, 34.363, 194.135 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 1.900 |
R-factor | 0.214 |
Rwork | 0.214 |
R-free | 0.26900 |
RMSD bond length | 0.006 |
RMSD bond angle | 17.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 15.000 |
High resolution limit [Å] | 1.900 |
Rmerge | 0.055 |
Number of reflections | 3749 |
Completeness [%] | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | drop was eluted 1:1 with a reservoir solution * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | |
4 | 1 | reservoir | PEG4000 | 30 (%) |