4UP2
Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-09-25 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 158.240, 158.240, 387.766 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.014 - 2.780 |
R-factor | 0.217 |
Rwork | 0.215 |
R-free | 0.24570 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2c44 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.696 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.010 | 2.880 |
High resolution limit [Å] | 2.780 | 2.780 |
Rmerge | 0.175 | 0.210 |
Number of reflections | 72775 | |
<I/σ(I)> | 25.72 | 2.54 |
Completeness [%] | 99.9 | 100 |
Redundancy | 42.6 | 43.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 25% PEG 4000 30MM AMMONIUM SULFATE 20MM B-MERCAPTOETHANOL 100MM TRIS-HCL PH 9 |