1I1W
0.89A Ultra high resolution structure of a Thermostable Xylanase from Thermoascus Aurantiacus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X9B |
| Synchrotron site | NSLS |
| Beamline | X9B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-04-03 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.050, 66.990, 50.760 |
| Unit cell angles | 90.00, 113.50, 90.00 |
Refinement procedure
| Resolution | 10.000 - 0.890 |
| Rwork | 0.090 |
| R-free | 0.10610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | LOCALLY AVAILABLE INTERMEDIATE REFINED ROOM TEMP. 1.11 A MODEL |
| RMSD bond length | 0.036 * |
| RMSD bond angle | 2.540 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.000 | 0.920 |
| High resolution limit [Å] | 0.890 | 0.890 |
| Rmerge | 0.047 | 0.180 |
| Total number of observations | 858643 * | |
| Number of reflections | 177476 | |
| <I/σ(I)> | 32.65 | 7.82 |
| Completeness [%] | 92.0 | 83 |
| Redundancy | 4.80 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.2 | 293 | Viswamitra, M.A., (1993) J.Mol.Biol., 232, 987. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 1 (%) | |
| 2 | 1 | drop | PEG6000 | 10 (%(w/v)) | |
| 3 | 1 | reservoir | PEG6000 | 50 (%) |
