2V9E
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)
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 21 2 |
Unit cell lengths | 107.520, 107.520, 115.017 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.880 - 1.580 |
R-factor | 0.159 |
Rwork | 0.158 |
R-free | 0.17600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.011 |
RMSD bond angle | 1.396 |
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] | 50.000 | |
High resolution limit [Å] | 1.580 | 1.580 |
Rmerge | 0.060 | 0.330 |
Number of reflections | 91205 | |
<I/σ(I)> | 19.33 | 5.96 |
Completeness [%] | 98.6 | 99.8 |
Redundancy | 8.2 | 8.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.2 | 40% (V/V) PEG 400, 0.1M HEPES (PH 7.5), 0.2 M CALCIUM ACETATE |