7MIE
Crystal structure of the Borreliella burgdorferi PlzA protein in complex with c-di-GMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-11-15 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 63.699, 36.861, 64.905 |
| Unit cell angles | 90.00, 113.90, 90.00 |
Refinement procedure
| Resolution | 32.260 - 1.600 |
| R-factor | 0.1921 |
| Rwork | 0.191 |
| R-free | 0.21760 |
| Structure solution method | SAD |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.716 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 32.260 | 50.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 4.340 | 1.600 |
| Rmerge | 0.086 | 0.062 | 0.573 |
| Rmeas | 0.095 | 0.068 | 0.635 |
| Rpim | 0.040 | 0.028 | 0.268 |
| Number of reflections | 35870 | 1905 | 1619 |
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 97.7 | 98.4 | 89.3 |
| Redundancy | 5.7 | 5.9 | 4.5 |
| CC(1/2) | 0.995 | 0.871 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 0.1 M succinic acid pH 7.0, 15% (w/v) PEG 3350 |






