4XUV
Crystal structure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E DW |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-12-09 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.5418 |
Spacegroup name | I 4 |
Unit cell lengths | 126.258, 126.258, 117.307 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.759 - 2.050 |
R-factor | 0.1921 |
Rwork | 0.191 |
R-free | 0.22210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3pmm 1nc5 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.662 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.090 |
High resolution limit [Å] | 2.050 | 2.050 |
Number of reflections | 57560 | |
<I/σ(I)> | 16.86 | 2.18 |
Completeness [%] | 100.0 | 100 |
Redundancy | 8.2 | 8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | 1 M potassium/sodium phosphate, trypsin protease cryo: 12% (w/v) glycerol then paratone-N oil |