2V9I
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-L274stop)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MARRESEARCH |
Spacegroup name | P 4 |
Unit cell lengths | 85.207, 85.207, 90.535 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.940 - 1.800 |
R-factor | 0.209 |
Rwork | 0.208 |
R-free | 0.23800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.021 |
RMSD bond angle | 1.875 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.060 | 0.370 |
Number of reflections | 55999 | |
<I/σ(I)> | 7.87 | 2.32 |
Completeness [%] | 93.5 | 94.9 |
Redundancy | 3.8 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.4 | 40% ETHYLENE GLYCOLE, 0.1M TRIS (PH 7.0) |