1CRU
SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE FROM ACINETOBACTER CALCOACETICUS IN COMPLEX WITH PQQ AND METHYLHYDRAZINE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-04-05 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 60.579, 92.658, 85.727 |
Unit cell angles | 90.00, 105.37, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.176 |
Rwork | 0.174 |
R-free | 0.19500 |
RMSD bond length | 0.027 * |
RMSD bond angle | 2.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.034 | 0.340 |
Total number of observations | 580379 * | |
Number of reflections | 142076 | |
<I/σ(I)> | 30.2 | |
Completeness [%] | 97.8 | 91.2 |
Redundancy | 4.1 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 9.2 | 293 | Oubrie, A., (1999) J.Mol.Biol., 289, 319. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | PQQ | 0.1 (mM) | |
3 | 1 | drop | PEG6000 | 8 (%(w/v)) | |
4 | 1 | drop | Tris-glycine | 50 (mM) | |
5 | 1 | reservoir | PEG6000 | 20-23 (%(w/v)) | |
6 | 1 | reservoir | 120 (mM) | ||
7 | 1 | reservoir | 3 (mM) | ||
8 | 1 | reservoir | Tris-glycine | 50 (mM) |