7WH7
The mutant crystal structure of b-1,4-Xylanase (XynAF1_N179S) with xylotetraose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-11-22 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.318, 119.687, 60.906 |
| Unit cell angles | 90.00, 102.20, 90.00 |
Refinement procedure
| Resolution | 16.960 - 1.440 |
| R-factor | 0.1507 |
| Rwork | 0.150 |
| R-free | 0.17150 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6jdt |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.906 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-2000 |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.490 |
| High resolution limit [Å] | 1.440 | 3.100 | 1.440 |
| Rmerge | 0.093 | 0.057 | 0.510 |
| Rmeas | 0.101 | 0.061 | 0.552 |
| Rpim | 0.038 | 0.024 | 0.210 |
| Total number of observations | 945941 | ||
| Number of reflections | 138872 | 13966 | 13885 |
| <I/σ(I)> | 5.5 | ||
| Completeness [%] | 99.9 | 99.3 | 100 |
| Redundancy | 6.8 | 6.7 | 6.8 |
| CC(1/2) | 0.995 | 0.895 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M BIS-TRIS pH 6.5, 25% w/v Polyethylene glycol 3350 |
