1K32
Crystal structure of the tricorn protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-12-10 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.939 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 95.860, 245.998, 159.040 |
Unit cell angles | 90.00, 105.30, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.248 * |
Rwork | 0.245 |
R-free | 0.25900 * |
Structure solution method | MIR+MAD+NCS Averaging |
RMSD bond length | 0.080 * |
RMSD bond angle | 1.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.208 * | 0.313 |
Number of reflections | 394093 | |
<I/σ(I)> | 6.7 | 1.9 |
Completeness [%] | 82.8 | 68.1 |
Redundancy | 2 | 1.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 20 * | 25% isopropanol, 0.1 M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | MES | 25-30 (%) | pH6.0 |