5Z49
Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose-1,5-bisphosphate
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-01-15 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97914 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.570, 86.700, 87.180 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.350 - 2.148 |
R-factor | 0.1908 |
Rwork | 0.188 |
R-free | 0.24060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5y2v |
RMSD bond length | 0.008 |
RMSD bond angle | 1.148 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.960 |
High resolution limit [Å] | 1.890 | 1.890 |
Number of reflections | 26386 | |
<I/σ(I)> | 14.68 | |
Completeness [%] | 99.3 | |
Redundancy | 4.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 289 | 0.1 M Tris pH 8.5, 25% tert-butanol |