6F2H
Structure of Protease 1 from Pyrococcus horikoshii co-crystallized in presence of 10 mM Tb-Xo4 and potassium iodide.
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 | 2015-10-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.6492 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 82.577, 84.698, 144.343 |
Unit cell angles | 90.00, 90.97, 90.00 |
Refinement procedure
Resolution | 46.010 - 2.190 |
R-factor | 0.152 |
Rwork | 0.150 |
R-free | 0.19300 |
RMSD bond length | 0.010 |
RMSD bond angle | 0.910 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | autoSHARP |
Refinement software | BUSTER (2.10.3) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.010 | |
High resolution limit [Å] | 2.190 | 2.190 |
Rpim | 0.072 | 0.447 |
Number of reflections | 101279 | |
<I/σ(I)> | 11.43 | |
Completeness [%] | 99.1 | |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 100 mM Bis tris propane pH 7, 20 to 30% PEG3350, Potassium Iodide 200 mM. Tb-Xo4 was directly mixed with the protein solution at a final concentration of 10 mM prior to crystallization. |