5D8G
A structural view on the dissociation of E. coli Tryptophanase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2010-04-14 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 118.287, 120.267, 171.709 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.200 - 1.890 |
R-factor | 0.17629 |
Rwork | 0.174 |
R-free | 0.21400 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.028 |
RMSD bond angle | 2.035 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.200 | |
High resolution limit [Å] | 1.890 | 1.890 |
Number of reflections | 45940 | |
<I/σ(I)> | 10.2 | |
Completeness [%] | 99.0 | |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 30%(w/v) PEG 400, 100 mM HEPES pH 7.5, 200 mM MgCl2, 5 mM 2-mercaptoethanol |