3FBQ
The crystal structure of the conserved domain protein from Bacillus anthracis
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9794, 0.9796 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 101.406, 101.406, 101.406 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 71.800 - 2.710 |
| R-factor | 0.20952 |
| Rwork | 0.206 |
| R-free | 0.28285 |
| Structure solution method | MAD |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.556 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 71.800 | 2.770 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.127 | 0.795 |
| Number of reflections | 9226 | |
| <I/σ(I)> | 21.45 | 2.72 |
| Completeness [%] | 99.6 | 97.41 |
| Redundancy | 8.5 | 8.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 2M (NH4)2SO4, 0.1M Tris and 0.2M Li2SO4, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
