3CLW
Crystal structure of conserved exported protein from Bacteroides fragilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-02-15 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97958 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 87.530, 116.258, 393.350 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.199 |
R-factor | 0.201 |
Rwork | 0.199 |
R-free | 0.24300 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.412 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | SHELXCD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.320 |
High resolution limit [Å] | 2.199 | 2.199 |
Rmerge | 0.101 | 0.551 |
Total number of observations | 129542 | |
Number of reflections | 172557 | |
<I/σ(I)> | 14.8 | 3 |
Completeness [%] | 84.5 | 79.5 |
Redundancy | 5.3 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7 | 294 | 200mM Sodium sulfate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, temperature 294K |