3BS3
Crystal structure of a putative DNA-binding protein from Bacteroides fragilis
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 | 2007-11-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97931, 0.97945 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 63.337, 63.337, 34.706 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.320 - 1.650 |
| R-factor | 0.185 |
| Rwork | 0.183 |
| R-free | 0.21900 |
| Structure solution method | MAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.346 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.690 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.094 | 0.509 |
| Number of reflections | 9728 | |
| <I/σ(I)> | 9.2 | 2.9 |
| Completeness [%] | 98.0 | 98 |
| Redundancy | 11.9 | 10 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | 0.1M Tris-HCl pH 8.5, 0.2M LiSO4, 1.25M (NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
