7WH6
The mutant crystal structure of b-1,4-Xylanase (XynAF1_N179S)
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 | 2020-12-03 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.297, 119.139, 60.828 |
| Unit cell angles | 90.00, 102.28, 90.00 |
Refinement procedure
| Resolution | 19.800 - 1.580 |
| R-factor | 0.1561 |
| Rwork | 0.155 |
| R-free | 0.18090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6jdt |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.699 |
| 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 | 1.640 |
| High resolution limit [Å] | 1.580 | 3.400 | 1.580 |
| Rmerge | 0.124 | 0.070 | 0.498 |
| Rmeas | 0.136 | 0.077 | 0.545 |
| Rpim | 0.056 | 0.032 | 0.220 |
| Total number of observations | 613650 | ||
| Number of reflections | 104905 | 10528 | 10491 |
| <I/σ(I)> | 4.2 | ||
| Completeness [%] | 99.9 | 99 | 100 |
| Redundancy | 5.8 | 5.6 | 5.9 |
| CC(1/2) | 0.991 | 0.771 |
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 |
