1GLO
Crystal Structure of Cys25Ser mutant of human cathepsin S
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH3R |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 79.989, 79.989, 61.517 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.197 * |
| Rwork | 0.193 |
| R-free | 0.25100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mem |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.754 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.075 | 0.270 |
| Total number of observations | 39038 * | |
| Number of reflections | 11969 | |
| <I/σ(I)> | 16 | 4.5 |
| Completeness [%] | 99.4 | 98.8 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.13 * | CRYSTALLISATION WAS PERFORMED BY THE HANGING-DROP VAPOUR DIFFUSION METHOD. EQUAL VOLUMES CATHEPSIN S (CYS25SER) AT 7 MG/ML, INCLUDING THE PEPTIDE ABZ-LEU-THR-BAL-HYP-TYR(NO2)-ASP-NH2 AT 1 MM AND WELL SOLUTION WERE COMBINED AND PLACED OVER A WELL CONTAINING 20% ISOPROPANOL, 20% PEG2000 AND 0.1M SODIUM CITRATE, PH 4.13 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | cathepsinS | 7 (mg/ml) | |
| 2 | 1 | drop | peptide | 1 (mM) | |
| 3 | 1 | reservoir | 2-propanol | 20 (%) | |
| 4 | 1 | reservoir | PEG2000 | 20 (%) | |
| 5 | 1 | reservoir | sodium citrate | 0.1 (M) | pH4.13 |
