5ZO0
Neutron structure of xylanase at pD5.4
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 | 2017-10-01 |
| Detector | BIODIFF |
| Wavelength(s) | 2.66 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.700, 60.026, 70.592 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.864 - 1.648 |
| R-factor | 0.1885 |
| Rwork | 0.186 |
| R-free | 0.22910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dfc |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.015 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.700 |
| High resolution limit [Å] | 1.650 | 3.780 | 1.650 |
| Rmerge | 0.133 | 0.047 | 0.558 |
| Rmeas | 0.170 | 0.057 | 0.752 |
| Rpim | 0.103 | 0.032 | 0.500 |
| Total number of observations | 44926 | ||
| Number of reflections | 22574 | 2022 | 1728 |
| <I/σ(I)> | 7.1 | ||
| Completeness [%] | 86.1 | 85.8 | 80.6 |
| Redundancy | 2 | 2.9 | 1.6 |
| CC(1/2) | 0.978 | 0.445 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 295 | 0.1M Tris, 0.1M NaCl, 1mM DTT, pH8.0, 2% PEG 3350, 0.2M NaI |
