7WHA
The mutant crystal structure of b-1,4-Xylanase (XynAF1_R246K)
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 PILATUS 6M |
| Wavelength(s) | 0.97914 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 68.165, 85.939, 97.831 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.300 - 1.830 |
| R-factor | 0.1552 |
| Rwork | 0.154 |
| R-free | 0.18310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6jdt |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.647 |
| 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 | 1.900 |
| High resolution limit [Å] | 1.830 | 3.940 | 1.830 |
| Rmerge | 0.105 | 0.050 | 0.480 |
| Rmeas | 0.109 | 0.053 | 0.500 |
| Rpim | 0.030 | 0.015 | 0.138 |
| Total number of observations | 676674 | ||
| Number of reflections | 51300 | 5408 | 5032 |
| <I/σ(I)> | 8 | ||
| Completeness [%] | 100.0 | 99.8 | 100 |
| Redundancy | 13.2 | 12.5 | 13 |
| CC(1/2) | 0.999 | 0.958 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2M Sodium formate, 20% w/v Polyethylene glycol 3350 |
