1XC4
Crystal structure of wild-type tryptophan synthase alpha-subunits from Escherichia coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-08-05 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54180 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 162.273, 44.479, 71.519 |
Unit cell angles | 90.00, 106.56, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.800 |
R-factor | 0.26 |
Rwork | 0.244 |
R-free | 0.31800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bks |
RMSD bond length | 0.006 |
RMSD bond angle | 1.265 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.900 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.139 | 0.321 |
Number of reflections | 12425 | |
<I/σ(I)> | 15.1 | |
Completeness [%] | 90.8 | 90.8 |
Redundancy | 9.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | ammonium sulfate, trisodium citrate dihydrate, lithium sulfate monohydrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |