2OXL
Structure and Function of the E. coli Protein YmgB: a Protein Critical for Biofilm Formation and Acid Resistance
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-25 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9790, 0.9793, 0.9322 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 69.919, 69.945, 55.021 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.21567 |
| Rwork | 0.215 |
| R-free | 0.23789 |
| Structure solution method | MAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.666 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE (2.11) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.038 | 0.403 |
| Number of reflections | 12802 | |
| <I/σ(I)> | 22.8 | |
| Completeness [%] | 99.6 | 96.8 |
| Redundancy | 6.6 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 8 | 295 | 90 mM Tris, 1.8 M NaCl, 0.5 (w/v)% B-OG, pH 8.0, microbatch, temperature 295K |
| 1 | MICROBATCH | 8 | 295 | 90 mM Tris, 1.8 M NaCl, 0.5 (w/v)% B-OG, pH 8.0, microbatch, temperature 295K |
| 1 | MICROBATCH | 8 | 295 | 90 mM Tris, 1.8 M NaCl, 0.5 (w/v)% B-OG, pH 8.0, microbatch, temperature 295K |






