1OJX
Crystal structure of an Archaeal fructose 1,6-bisphosphate aldolase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X13 |
Temperature [K] | 100 |
Collection date | 2002-02-15 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.300, 158.974, 102.986 |
Unit cell angles | 90.00, 108.11, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.900 |
R-factor | 0.15 |
Rwork | 0.149 |
R-free | 0.17900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 * |
RMSD bond angle | 1.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.085 | 0.365 |
Number of reflections | 188245 | |
<I/σ(I)> | 14.5 | 2.4 |
Completeness [%] | 94.5 | 87 |
Redundancy | 4 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | 20 * | 9% (W/V) PEG 4000, 0.1 M NAACETATE PH 5.0, 1-8% GLYCEROL |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | drop | HEPES-NaOH | 10 (mM) | pH7.5 |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | reservoir | PEG4000 | 9 (%(w/v)) | |
6 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.0 |