6SHU
Borrelia burgdorferi BmpD nucleoside binding protein bound to adenosine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-04-30 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 106.780, 42.900, 66.380 |
| Unit cell angles | 90.00, 117.34, 90.00 |
Refinement procedure
| Resolution | 30.705 - 1.430 |
| R-factor | 0.154848832023 |
| Rwork | 0.154 |
| R-free | 0.17934 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.806 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 58.970 | 1.481 |
| High resolution limit [Å] | 1.430 | 1.430 |
| Rmerge | 0.062 | 0.316 |
| Rmeas | 0.067 | 0.355 |
| Number of reflections | 44945 | 2652 |
| <I/σ(I)> | 19.34 | 3.86 |
| Completeness [%] | 92.0 | 51.3 |
| Redundancy | 7.6 | 4.9 |
| CC(1/2) | 0.999 | 0.915 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 294.15 | 0.2 M CaCl2, 0.1 M NaAcetate pH 5.0, 20 % PEG6000 |
