4A05
Structure of the catalytic core domain of the cellobiohydrolase, Cel6A, from Chaetomium thermophilum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04-1 |
Synchrotron site | Diamond |
Beamline | I04-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-22 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.710, 76.060, 107.240 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.030 - 1.900 |
R-factor | 0.16875 |
Rwork | 0.167 |
R-free | 0.19722 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1oc6 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.222 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0086) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.090 | 0.200 |
Number of reflections | 32910 | |
<I/σ(I)> | 14.6 | 7.4 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 7.1 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 20% PEG 6000, 0.1M HEPES PH 7.0, 0.14 M LICL |