2YCE
Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.
Replaces: 1W8RExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 82.900, 159.200, 101.400 |
| Unit cell angles | 90.00, 107.80, 90.00 |
Refinement procedure
| Resolution | 39.800 - 1.930 |
| R-factor | 0.15654 |
| Rwork | 0.156 |
| R-free | 0.19811 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ojx |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.485 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.020 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.080 | 0.370 |
| Number of reflections | 179009 | |
| <I/σ(I)> | 16.2 | 2.2 |
| Completeness [%] | 97.3 | 77.6 |
| Redundancy | 4.2 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 9% (W/V) PEG 4000, 0.1 M NAACETATE PH 5.0, 1-8% GLYCEROL, 100 MM FBP |
