2IX9
Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-12 |
| Detector | ADSC CCD |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 158.825, 51.556, 72.553 |
| Unit cell angles | 90.00, 109.27, 90.00 |
Refinement procedure
| Resolution | 74.950 - 1.700 |
| R-factor | 0.155 |
| Rwork | 0.153 |
| R-free | 0.19000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hl6 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.383 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.000 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.090 | 0.450 |
| Number of reflections | 60965 | |
| <I/σ(I)> | 13.8 | 2.3 |
| Completeness [%] | 98.6 | 90.9 |
| Redundancy | 4.6 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9.5 | 1.8 M AMMONIUM SULPHATE 0.2 M LITHIUM SULPHATE 0.1 M CAPS PH 9.5 |
