1I1X
1.11 A ATOMIC 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] | 293 |
| Detector technology | CCD |
| Collection date | 1999-02-28 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.009 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.520, 68.090, 51.440 |
| Unit cell angles | 90.00, 113.56, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.110 |
| Rwork | 0.099 |
| R-free | 0.12360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1TUX (1.8 A) |
| RMSD bond length | 0.016 |
| RMSD bond angle | 2.100 * |
| 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] | 25.000 | 1.150 |
| High resolution limit [Å] | 1.110 | 1.110 |
| Rmerge | 0.052 | 0.360 |
| Total number of observations | 294946 * | |
| Number of reflections | 90855 | |
| <I/σ(I)> | 20.6 | 3 |
| Completeness [%] | 87.5 | 81.3 |
| Redundancy | 3.25 * |
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 (%) |
