2V9N
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A88F- 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 | C 1 2 1 |
Unit cell lengths | 168.379, 106.417, 106.564 |
Unit cell angles | 90.00, 126.76, 90.00 |
Refinement procedure
Resolution | 51.030 - 1.400 |
R-factor | 0.167 |
Rwork | 0.166 |
R-free | 0.18700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.008 |
RMSD bond angle | 1.175 |
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] | 51.000 | |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.080 | 0.340 |
Number of reflections | 268317 | |
<I/σ(I)> | 7.25 | 2.88 |
Completeness [%] | 91.0 | 94.4 |
Redundancy | 2.3 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.9 | 25% (V/V) 1,2-PROPANEDIOL, 10% (V/V) GLYCEROL, 5% (W/V) PEG 3000, PHOSPHATE-CITRATE BUFFER (0.1M, PH 4.2) |