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 |