2PLX
Trypsin complexed to a synthetic peptide from Veronica hederifolia
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.1 |
| Synchrotron site | SRS |
| Beamline | PX14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-01-23 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.488 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 113.558, 41.521, 51.189 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 56.800 - 1.560 |
| R-factor | 0.145 |
| Rwork | 0.143 |
| R-free | 0.18800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sfi |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.738 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (refmac_5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.800 | 1.620 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.044 | 0.611 |
| Number of reflections | 28405 | |
| <I/σ(I)> | 20.7 | |
| Completeness [%] | 80.2 | 11.5 |
| Redundancy | 3.8 | 1.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291.15 | 1.3-1.5M Na Citrate, 0.1M Na Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.15K |
