1R52
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.934 |
Spacegroup name | P 1 |
Unit cell lengths | 57.816, 75.599, 91.327 |
Unit cell angles | 114.44, 108.43, 89.98 |
Refinement procedure
Resolution | 29.700 * - 2.890 |
R-factor | 0.18981 |
Rwork | 0.188 |
R-free | 0.22400 * |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 1.460 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | |
High resolution limit [Å] | 2.900 * | |
Rmerge | 0.040 | 0.300 * |
Total number of observations | 110781 * | |
Number of reflections | 26514 * | |
<I/σ(I)> | 21.5 | |
Completeness [%] | 90.0 | 62.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Na-citrate, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | reservoir | sodium cirtate | 0.7 (M) | |
3 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |