5VXO
Crystal Structure Analysis of human CLYBL in complex with propionyl-CoA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-09-12 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.999973 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.589, 131.841, 82.440 |
| Unit cell angles | 90.00, 93.05, 90.00 |
Refinement procedure
| Resolution | 82.323 - 2.266 |
| R-factor | 0.1771 |
| Rwork | 0.174 |
| R-free | 0.23130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5vxc |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.221 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 82.323 | 82.323 | 2.274 |
| High resolution limit [Å] | 2.266 | 10.512 | 2.266 |
| Rmerge | 0.096 | 0.034 | 0.732 |
| Rmeas | 0.113 | 0.041 | 0.854 |
| Rpim | 0.059 | 0.022 | 0.437 |
| Total number of observations | 174831 | 1815 | 1959 |
| Number of reflections | 47726 | ||
| <I/σ(I)> | 11.1 | 30.4 | 2 |
| Completeness [%] | 97.3 | 98.6 | 99.6 |
| Redundancy | 3.7 | 3.6 | 3.8 |
| CC(1/2) | 0.995 | 0.989 | 0.639 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 293 | 1 uL protein at 4 mg/ml and well solution (0.1 M Na2HPO4:citric acid pH 4.2, 40% (v/v) PEG 300) |
