2F9N
Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant K192Q/D216G in Complex with Leupeptin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-07-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 83.310, 88.570, 163.370 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.900 - 1.600 |
| R-factor | 0.19 |
| Rwork | 0.190 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lto |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.900 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.060 | 0.477 |
| Number of reflections | 156713 | |
| <I/σ(I)> | 23.8 | |
| Completeness [%] | 98.8 | 92.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.8 | 293 | 28% PEG 1500, pH 6.80, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
