1GVF
Structure of tagatose-1,6-bisphosphate aldolase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | MAR, RAXIS |
Wavelength(s) | 1.282,1.283,1.127,1.030, 1.5418,0.933 |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 72.650, 100.460, 206.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.450 |
R-factor | 0.17 * |
R-free | 0.13000 * |
Structure solution method | DIRECT METHODS |
RMSD bond length | 0.018 |
RMSD bond angle | 0.030 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | RSPS |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.800 | 1.480 |
High resolution limit [Å] | 1.450 | 1.450 |
Rmerge | 0.064 | 0.292 |
Total number of observations | 1086028 * | |
Number of reflections | 131455 * | |
<I/σ(I)> | 15 | 1.5 |
Completeness [%] | 98.4 | 97.9 |
Redundancy | 3 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 20 * | pH 6.40 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 6.5 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.5 |
3 | 1 | drop | PGH | 20 (mM) | |
4 | 1 | reservoir | ethylene glycol | 7-12 (%(v/v)) | |
5 | 1 | reservoir | 10 (mM) | ||
6 | 1 | reservoir | sodium cacodylate | 42 (mM) | pH6.4 |