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 |