2P86
The high resolution crystal structure of rhodesain, the major cathepsin L protease from T. brucei rhodesiense, bound to inhibitor K11002
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-20 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 33.659, 78.628, 80.725 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.360 - 1.160 |
| R-factor | 0.111 |
| Rwork | 0.110 |
| R-free | 0.13000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2p7u WITHOUT WATERS OR SMALL MOLECULE INHIBITOR |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.876 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.360 | 1.220 |
| High resolution limit [Å] | 1.160 | 1.160 |
| Rmerge | 0.043 | 0.120 |
| Number of reflections | 68633 | |
| <I/σ(I)> | 27.2 | 14.9 |
| Completeness [%] | 91.9 | 80 |
| Redundancy | 7.1 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 298 | 1.6M Ammonium Sulfate, 0.1 M Bicine pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
