3RPJ
Structure of a curlin genes transcriptional regulator protein from Proteus mirabilis HI4320.
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 | 2009-11-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97904 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.380, 77.952, 86.163 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.980 - 1.900 |
| R-factor | 0.184 |
| Rwork | 0.182 |
| R-free | 0.21120 |
| Structure solution method | SAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.339 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 5.160 | 1.900 |
| Rmerge | 0.084 | 0.080 | 0.579 |
| Number of reflections | 27263 | ||
| <I/σ(I)> | 8.4 | ||
| Completeness [%] | 99.8 | 97.7 | 99.5 |
| Redundancy | 9.1 | 8.1 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 297 | 0.1M Bis-Tris propane, 2.0M Ammonium Sulfate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K |
