6EQO
Tri-functional propionyl-CoA synthase of Erythrobacter sp. NAP1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-07-13 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 383.414, 86.740, 133.958 |
| Unit cell angles | 90.00, 108.89, 90.00 |
Refinement procedure
| Resolution | 46.179 - 2.700 |
| R-factor | 0.1914 |
| Rwork | 0.191 |
| R-free | 0.22890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.765 |
| Data reduction software | iMOSFLM (7.0) |
| Data scaling software | Aimless (0.5.26) |
| Phasing software | PHENIX |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 46.180 | 46.180 | 2.750 |
| High resolution limit [Å] | 2.700 | 14.790 | 2.700 |
| Rmerge | 0.212 | 0.114 | 0.886 |
| Rmeas | 0.255 | 0.135 | 1.092 |
| Rpim | 0.140 | 0.072 | 0.626 |
| Total number of observations | 349063 | 2516 | 14441 |
| Number of reflections | 112000 | 736 | 5260 |
| <I/σ(I)> | 4.2 | 8.3 | 1.7 |
| Completeness [%] | 97.9 | 96.6 | 94.2 |
| Redundancy | 3.1 | 3.4 | 2.7 |
| CC(1/2) | 0.958 | 0.963 | 0.189 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.9 | 291 | 1 part protein solution (10 mg/mL protein in 20 mM Tris-HCl, pH 7.9, 150 mM sodium chloride, 2 mM CoA, 2 mM NADP+, 2 mM beta,gamma-methylene-ATP) + 1 part buffer (0.1 M BisTris, pH 6.5, 0.2 M sodium acetate, 25% w/v PEG3350, 3% w/v trimethylamine N-oxide dihydrate) |
