3S2C
Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila RKU-1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LNLS BEAMLINE W01B-MX2 |
Synchrotron site | LNLS |
Beamline | W01B-MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-05-10 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.4586 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 105.950, 187.292, 180.636 |
Unit cell angles | 90.00, 90.87, 90.00 |
Refinement procedure
Resolution | 49.240 - 3.000 |
R-factor | 0.198 |
Rwork | 0.195 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pz3 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.389 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Number of reflections | 137481 | |
Completeness [%] | 97.9 | 97 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |