2C44
Crystal Structure of E. coli Tryptophanase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2002-07-31 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 215.510, 215.510, 107.560 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 500.000 - 2.800 |
R-factor | 0.164 |
Rwork | 0.196 |
R-free | 0.22000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ax4 |
RMSD bond length | 0.031 |
RMSD bond angle | 2.683 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 500.000 | 2.910 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.090 | 0.240 |
Number of reflections | 62257 | |
<I/σ(I)> | 26.9 | 8.7 |
Completeness [%] | 99.3 | 98.8 |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.9 | 1.6M AMMONIUM SULFATE, 0.5%(V/V)PEG400, 0.1M SODIUM HEPES PH 7.9 |