5EBA
Crystal structure of aromatic mutant (Y343A) of an alkali thermostable GH10 xylanase from Bacillus sp. NG-27
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2010-09-03 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 73.860, 80.110, 69.210 |
| Unit cell angles | 90.00, 111.19, 90.00 |
Refinement procedure
| Resolution | 64.530 - 2.300 |
| R-factor | 0.1807 |
| Rwork | 0.178 |
| R-free | 0.23490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2f8q |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.095 |
| Data reduction software | SCALA |
| Data scaling software | SCALA (3.3.21) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 64.531 | 34.032 | 2.420 |
| High resolution limit [Å] | 2.300 | 7.270 | 2.300 |
| Rmerge | 0.041 | 0.218 | |
| Rmeas | 0.069 | ||
| Rpim | 0.034 | 0.023 | 0.130 |
| Total number of observations | 58295 | 2031 | 8236 |
| Number of reflections | 15361 | ||
| <I/σ(I)> | 14.3 | 27.9 | 5.1 |
| Completeness [%] | 91.9 | 96.5 | 93.8 |
| Redundancy | 3.8 | 3.8 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 8.5 | 293 | 0.1M NaCl, 150mM MgCl2, 0.1M Tris-HCl pH 8.5, 15% PEG 6000 |
