2V3Q
Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein
Replaces: 2CAPExperimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.934, 0.7228, 0.718758 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 96.245, 86.843, 89.889 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.950 - 1.890 |
| R-factor | 0.13 |
| Rwork | 0.127 |
| R-free | 0.18600 |
| Structure solution method | SIRAS |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.142 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.000 | 2.010 |
| High resolution limit [Å] | 1.900 | 1.890 |
| Rmerge | 0.090 | 0.230 |
| Number of reflections | 30194 | |
| <I/σ(I)> | 13.78 | 7.31 |
| Completeness [%] | 99.4 | 91.8 |
| Redundancy | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 50MM CACODYLATE BUFFER PH 6, AMMONIUM SULFATE 2M AND SODIUM CHLORIDE 1MM |
