1F9Z
CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 200 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-30 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.047, 56.478, 46.705 |
Unit cell angles | 90.00, 95.44, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.205 * |
Rwork | 0.205 |
R-free | 0.27200 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.987 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SHARP |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.570 |
High resolution limit [Å] | 1.500 | 1.490 |
Rmerge | 0.069 | 0.290 |
Total number of observations | 116872 * | |
Number of reflections | 38619 | |
<I/σ(I)> | 12.8 | |
Completeness [%] | 99.0 | 98 |
Redundancy | 3.5 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 277 | PEG1000, PEG8000, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12-37 (mg/ml) | |
2 | 1 | reservoir | PEG1000 | 5-10 (%) | |
3 | 1 | reservoir | PEG8000 | 5-10 (%) |