3C1U
D192N mutant of Rhamnogalacturonan acetylesterase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-05-25 |
Detector | MARRESEARCH |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.612, 67.606, 73.272 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.330 |
R-factor | 0.115 |
Rwork | 0.114 |
R-free | 0.15300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k7c |
RMSD bond length | 0.013 |
RMSD bond angle | 0.030 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | EPMR |
Refinement software | SHELX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.350 |
High resolution limit [Å] | 1.330 | 1.330 |
Rmerge | 0.032 | 0.198 |
Number of reflections | 55818 | |
<I/σ(I)> | 31.8 | |
Completeness [%] | 99.5 | 98.3 |
Redundancy | 8.9 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3 | 298 | PEG1500, sodium acetate, pH3.0, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP |