2OQX
Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-01-01 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 118.422, 120.116, 171.209 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.820 - 1.900 |
R-factor | 0.21 |
Rwork | 0.203 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 1.200 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.070 | 0.310 |
Number of reflections | 88583 | |
<I/σ(I)> | 42.54 | 4.25 |
Completeness [%] | 95.4 | 99.3 |
Redundancy | 3.3 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 30% PEG 400, 100mM HEPES, 100 mM magnesium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |