3DEL
The structure of CT381, the arginine binding protein from the periplasm Chlamydia trachomatis
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 | 2008-02-21 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97995 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.072, 121.875, 170.097 |
Unit cell angles | 90.00, 95.38, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.920 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.21330 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.127 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.000 | 2.020 |
High resolution limit [Å] | 1.920 | 1.920 |
Rmerge | 0.086 | 0.480 |
Number of reflections | 123164 | |
<I/σ(I)> | 13.8 | 2.1 |
Completeness [%] | 99.5 | 96.6 |
Redundancy | 4.1 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 293 | Sodium Formate 0.5M-4M, Tris Base 100mM, pH 6.8-8.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |