2E24
crystal structure of a mutant (R612A) of xanthan lyase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.807, 90.230, 78.098 |
Unit cell angles | 90.00, 97.56, 90.00 |
Refinement procedure
Resolution | 46.900 - 2.150 |
R-factor | 0.175 |
Rwork | 0.175 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1x1h |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.113 | 0.324 |
Number of reflections | 39353 | |
Completeness [%] | 97.3 | 77.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 22% PEG 4000, 0.2M ammonium formate, 0.1M Sodium Bicine, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 293K |