3KR5
Structure of a protease 4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.95376 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 172.080, 174.160, 227.706 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 77.700 - 2.560 |
R-factor | 0.22288 |
Rwork | 0.220 |
R-free | 0.27766 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kqx |
RMSD bond length | 0.013 |
RMSD bond angle | 1.456 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 78.900 | 2.740 |
High resolution limit [Å] | 2.560 | 2.560 |
Rmerge | 0.549 | 1.299 |
Total number of observations | 2662653 | |
Number of reflections | 217885 | |
<I/σ(I)> | 4.1 | 2.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 12.2 | 12.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 40% PEG 400, 0.1M Tris pH 8.5, 0.2M LiSO4, 1mM TCEP, 1mM ZnCl2, 1mM Co4/BEY, VAPOR DIFFUSION, HANGING DROP, temperature 298K |