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 |
