7QO8
Structure of Protease1 from Pyrococcus horikoshii in space group 19 with a hexamer in the asymmetric unit
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-05-03 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9797 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 115.741, 123.636, 129.223 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.590 - 1.950 |
R-factor | 0.1818 |
Rwork | 0.181 |
R-free | 0.20400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6q3t |
RMSD bond length | 0.009 |
RMSD bond angle | 1.103 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.720 | 2.050 |
High resolution limit [Å] | 1.950 | 1.950 |
Rpim | 0.068 | 0.673 |
Number of reflections | 135285 | 19324 |
<I/σ(I)> | 11.8 | |
Completeness [%] | 99.8 | |
Redundancy | 6.6 | |
CC(1/2) | 0.997 | 0.567 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 100 mM tri-sodium citrate pH 5.6, 200 mM sodium potassium tartrate, 1.9 to 2.4 M Ammonium sulfate |