4KBR
Crystal structure of mouse Ceramide-1-phosphate transfer protein (apo-form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 81.997, 83.876, 268.721 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.507 - 2.547 |
| R-factor | 0.2042 |
| Rwork | 0.201 |
| R-free | 0.27090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Human CPTP in complex with 2:0 C1P |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.151 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.640 |
| High resolution limit [Å] | 2.550 | 5.490 | 2.550 |
| Rmerge | 0.086 | 0.032 | 0.596 |
| Number of reflections | 57653 | ||
| <I/σ(I)> | 8.3 | ||
| Completeness [%] | 93.5 | 99.8 | 85.4 |
| Redundancy | 10 | 9.8 | 10.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M Bis-Tris pH 6.5, 2 M Ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
