4B54
The Structure of the inactive mutant G153R of LptC from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2010-07-28 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 40.940, 98.280, 123.560 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.800 |
R-factor | 0.24155 |
Rwork | 0.240 |
R-free | 0.26551 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3my2 |
RMSD bond length | 0.006 |
RMSD bond angle | 0.914 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.120 | 0.720 |
Number of reflections | 12846 | |
<I/σ(I)> | 12.9 | 3.2 |
Completeness [%] | 99.5 | 99.4 |
Redundancy | 5.1 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.5 | STURA FOOTPRINT SCREEN NUMBER 1 CONDITION 18.2 (MOLECULAR DIMENSIONS) 18% PEG5K MME, 0.1M SODIUM ACETATE PH 5.5 PLUS 30% GLYCEROL FOR CRYOCOOLING |