2RA1
Crystal structure of the N-terminal part of the bacterial S-layer protein SbsC
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-10-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.200 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.645, 94.877, 59.646 |
| Unit cell angles | 90.00, 106.68, 90.00 |
Refinement procedure
| Resolution | 20.009 - 2.406 |
| Rwork | 0.177 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | N-terminal domains form the structure of rSbsC(31-844) |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.131 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 99.000 | 99.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 6.510 | 2.400 |
| Rmerge | 0.064 | 0.053 | 0.196 |
| Number of reflections | 20541 | ||
| <I/σ(I)> | 22.1 | ||
| Completeness [%] | 99.7 | 96.1 | 97.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | batch method | 6.5 | 298 | 6-14% PEG3350, various salts - NaCl, LiCl etc., pH 6.5, batch method, temperature 298K |
