2V29
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)
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 | 2003-10-14 |
Detector | MARRESEARCH |
Spacegroup name | P 4 |
Unit cell lengths | 82.873, 82.873, 98.109 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.220 - 2.000 |
R-factor | 0.164 |
Rwork | 0.161 |
R-free | 0.19700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ojr |
RMSD bond length | 0.015 |
RMSD bond angle | 1.351 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.080 | 0.040 |
Number of reflections | 44803 | |
<I/σ(I)> | 12.29 | 4.17 |
Completeness [%] | 100.0 | 100 |
Redundancy | 4.26 | 4.24 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.5 | 100 MM SODIUM ACETATE PH 4.5, 50% (V/V) ETHYLENEGLYCOL, 5% (V/V) PEG 1000 |