1H4W
Structure of human trypsin IV (brain trypsin)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2000-06-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 56.683, 56.683, 143.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 52.700 - 1.700 |
| R-factor | 0.188 |
| Rwork | 0.188 |
| R-free | 0.20300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1trn |
| RMSD bond length | 0.004 |
| RMSD bond angle | 25.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.700 | 1.740 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.049 | 0.323 |
| Total number of observations | 111768 * | |
| Number of reflections | 26174 | |
| <I/σ(I)> | 18.5 | 2.5 |
| Completeness [%] | 94.9 | 92 |
| Redundancy | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.7 | 298 | HANGING DROP VAPOUR DIFFUSION 3.3 MG/ML PROTEIN, 2% PEG 4000, 0.05M TRIS PH7.7, 2.5MM CACL2, 2.5 MG/ML BENZAMIDINE/HCL, 25 C, pH 7.70 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6.5 (mg/ml) | |
| 2 | 1 | drop | 10 (mM) | ||
| 3 | 1 | reservoir | PEG8000 | 4 (%(w/v)) | |
| 4 | 1 | reservoir | Tris | 0.1 (M) | pH7.7 |
| 5 | 1 | reservoir | 5 (mM) | ||
| 6 | 1 | reservoir | benzamidine/HCl | 5 (mg/ml) |
