5MO2
Neutron structure of cationic trypsin in complex with N-amidinopiperidine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | NUCLEAR REACTOR |
| Source details | FRM II BEAMLINE BIODIFF |
| Synchrotron site | FRM II |
| Beamline | BIODIFF |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Collection date | 2014-10-09 |
| Detector | MAATEL BIODIFF |
| Wavelength(s) | 2.673, 2.678 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.941, 58.636, 67.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.135 - 1.500 |
| R-factor | 0.163 |
| Rwork | 0.161 |
| R-free | 0.19990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4i8h |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.928 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((dev_2429)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.110 | 0.454 |
| Number of reflections | 31665 | |
| <I/σ(I)> | 7.525 | 2.182 |
| Completeness [%] | 88.7 | 79.9 |
| Redundancy | 3.1 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 0.2 M ammonium sulfate, 0.1 M Hepes pH 7.5, 16% (w/v) PEG 8000 |
