4DPK
Structure of malonyl-coenzyme A reductase from crenarchaeota
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9764 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 167.090, 81.940, 124.610 |
| Unit cell angles | 90.00, 104.95, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.050 |
| R-factor | 0.18695 |
| Rwork | 0.185 |
| R-free | 0.23069 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ys4 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.579 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Number of reflections | 107988 | |
| <I/σ(I)> | 13.8 | 2.8 |
| Completeness [%] | 91.1 | 56.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 34% MPD,0.1 M HEPES,100 mM CaCl2, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
