5MO1
Neutron structure of cationic trypsin in complex with benzylamine
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 | 2016-08-10 |
| Detector | MAATEL BIODIFF |
| Wavelength(s) | 2.673 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.017, 58.630, 67.753 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.680 - 1.491 |
| R-factor | 0.1775 |
| Rwork | 0.175 |
| R-free | 0.21600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4i8h |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.054 |
| 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 | 1.520 |
| High resolution limit [Å] | 1.490 | 1.490 |
| Rmerge | 0.129 | 0.445 |
| Number of reflections | 34022 | |
| <I/σ(I)> | 5.866 | 1.954 |
| Completeness [%] | 93.7 | 90.4 |
| Redundancy | 2.8 | 2.1 |
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, 15% (w/v) PEG 8000 |
