6HQC
Structural investigation of the TasA anchoring protein TapA from Bacillus subtilis
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-06 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.91841, 0.9795 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 30.103, 61.135, 34.291 |
| Unit cell angles | 90.00, 106.93, 90.00 |
Refinement procedure
| Resolution | 32.800 - 1.280 |
| R-factor | 0.14969 |
| Rwork | 0.147 |
| R-free | 0.19715 |
| Structure solution method | SAD |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.686 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | Auto-Rickshaw |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.800 | 1.390 |
| High resolution limit [Å] | 1.280 | 1.280 |
| Rmeas | 0.004 | 0.177 |
| Number of reflections | 30250 | |
| <I/σ(I)> | 14.19 | 0.85 |
| Completeness [%] | 98.4 | 97.2 |
| Redundancy | 4.44 | |
| CC(1/2) | 0.999 | 0.432 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.5 | 293 | 20% PEG MME 550, 0.1M NaCl, 0.1M Bicine pH 9.5 |
