3L18
Ton1285, an Intracellular Protease from Thermococcus onnurineus NA1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PAL/PLS BEAMLINE 4A |
Synchrotron site | PAL/PLS |
Beamline | 4A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 63 |
Unit cell lengths | 87.114, 87.114, 80.119 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.490 - 1.780 |
R-factor | 0.1628 |
Rwork | 0.160 |
R-free | 0.21451 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g2i |
RMSD bond length | 0.012 |
RMSD bond angle | 1.312 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 |
High resolution limit [Å] | 1.780 | 1.780 |
Number of reflections | 31234 | |
<I/σ(I)> | 5.9 | 4.23 |
Completeness [%] | 99.5 | |
Redundancy | 16.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 8 | 295 | 20% PEG 8000, 0.1M HEPES pH7.5, 0.2M Ammonium sulfate, pH 8.0, EVAPORATION, temperature 295K |