1FA8
CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF 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] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-20 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 46.275, 57.197, 46.990 |
Unit cell angles | 90.00, 95.24, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.700 |
R-factor | 0.188 * |
Rwork | 0.188 |
R-free | 0.25500 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.483 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | TNT |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.051 | 0.241 * |
Total number of observations | 81372 * | |
Number of reflections | 29051 | |
<I/σ(I)> | 11.5 | |
Completeness [%] | 97.8 | 93.1 |
Redundancy | 2.8 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 275 | PEG 1000, PEG 4000, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 275K |
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 (%) |