3CNE
Crystal structure of the putative protease I from Bacteroides thetaiotaomicron
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9794 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.607, 68.021, 75.389 |
Unit cell angles | 90.00, 109.81, 90.00 |
Refinement procedure
Resolution | 36.350 - 1.990 |
R-factor | 0.18839 |
Rwork | 0.186 |
R-free | 0.23441 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.424 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.045 |
High resolution limit [Å] | 1.990 | 1.990 |
Rmerge | 0.125 | 0.345 |
Number of reflections | 45132 | |
<I/σ(I)> | 17.54 | 3.77 |
Completeness [%] | 99.1 | 91.46 |
Redundancy | 5.2 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 0.2M CaCl2, 0.1M Tris-HCl pH 8.5, 25% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 289K |