1MA9
Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, Hamburg |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-09-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8423 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 74.440, 74.900, 88.020 |
| Unit cell angles | 90.00, 110.19, 90.00 |
Refinement procedure
| Resolution | 19.910 - 2.400 |
| R-factor | 0.2033 |
| Rwork | 0.200 |
| R-free | 0.25320 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 1ATN 1j78 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.162 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.042 | 0.250 |
| Total number of observations | 97747 * | |
| Number of reflections | 33252 * | |
| <I/σ(I)> | 12.2 | 1.8 |
| Completeness [%] | 93.3 | 93.9 |
| Redundancy | 2.9 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 277 | Verboven, C.C., (1995) J. Steroid Biochem. Mol. Biol., 54, 11. * |
