7WHE
The mutant crystal structure of b-1,4-Xylanase (XynAF1_R246K) with xylobiose
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 | 2019-12-06 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97914 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 68.056, 85.854, 97.701 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.110 - 1.750 |
| R-factor | 0.1531 |
| Rwork | 0.151 |
| R-free | 0.18450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6jdt |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.663 |
| 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 | 1.810 |
| High resolution limit [Å] | 1.750 | 3.770 | 1.750 |
| Rmerge | 0.148 | 0.084 | 0.470 |
| Rmeas | 0.154 | 0.087 | 0.490 |
| Rpim | 0.043 | 0.025 | 0.137 |
| Total number of observations | 764269 | ||
| Number of reflections | 58475 | 6144 | 5747 |
| <I/σ(I)> | 6 | ||
| Completeness [%] | 100.0 | 99.7 | 100 |
| Redundancy | 13.1 | 12.1 | 12.7 |
| CC(1/2) | 0.996 | 0.942 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2M Sodium formate, 20% w/v Polyethylene glycol 3350 |
