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 |
