3KR4
Structure of a protease 3
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 | 2009-07-08 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.95659 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 173.561, 178.121, 230.479 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.150 - 2.000 |
R-factor | 0.19459 |
Rwork | 0.192 |
R-free | 0.24193 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3kqx |
RMSD bond length | 0.018 |
RMSD bond angle | 1.628 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0063) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 62.140 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.251 | 0.999 |
Total number of observations | 6476290 | |
Number of reflections | 469417 | |
<I/σ(I)> | 11.3 | 2.5 |
Completeness [%] | 98.5 | 96.6 |
Redundancy | 13.8 | 11.8 |
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 MgCl2, 1mM Bestatin, VAPOR DIFFUSION, HANGING DROP, temperature 298K |