2V9O
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-15 |
Detector | MARRESEARCH |
Spacegroup name | P 4 |
Unit cell lengths | 86.193, 86.193, 89.873 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.950 - 1.950 |
R-factor | 0.206 |
Rwork | 0.203 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.024 |
RMSD bond angle | 2.267 |
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] | 45.000 | |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.060 | 0.380 |
Number of reflections | 47805 | |
<I/σ(I)> | 13.45 | 3.9 |
Completeness [%] | 99.7 | 100 |
Redundancy | 4.33 | 4.12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.3 | 50% (V/V) ETHYLENE GLYCOL, 0.1 M HEPES (PH 7.5), 0.2 M LITHIUM SULFATE |