1PPZ
Trypsin complexes at atomic and ultra-high resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, Hamburg |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-04-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8110 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.999, 66.505, 39.244 |
| Unit cell angles | 90.00, 108.67, 90.00 |
Refinement procedure
| Resolution | 35.000 - 1.220 * |
| Rwork | 0.141 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 31.000 * | 1.240 |
| High resolution limit [Å] | 1.220 | 1.220 |
| Rmerge | 0.045 * | |
| Number of reflections | 47457 * | |
| <I/σ(I)> | 28 | 5.5 |
| Completeness [%] | 99.6 | 97.7 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5 | 293 | Rypniewski, W.R., (1993) Protein Eng., 6, 341. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12.5 (mg/ml) | |
| 2 | 1 | drop | ammonium sulfate | 0.7 (M) | |
| 3 | 1 | drop | citrate | 50 (mM) | |
| 4 | 1 | reservoir | ammonium sulfate | 1.4 (M) | |
| 5 | 1 | reservoir | sodium citrate | 0.1 (M) |
