2V9G
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y- L84W-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 |
Detector | MARRESEARCH |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 87.902, 100.825, 270.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.960 - 2.700 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.25200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gt7 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | |
High resolution limit [Å] | 2.670 | 2.670 |
Rmerge | 0.110 | 0.380 |
Number of reflections | 32949 | |
<I/σ(I)> | 9.77 | 3.4 |
Completeness [%] | 95.2 | 85.6 |
Redundancy | 3.63 | 3.56 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.7 | 1 M NA/K-TARTRATE, 0.1 M HEPES (PH 7.7) |