1J78
Crystallographic analysis of the human vitamin D binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, Hamburg |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-04-17 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9116 |
Spacegroup name | P 43 |
Unit cell lengths | 132.248, 132.248, 73.179 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.380 - 2.310 |
R-factor | 0.2201 * |
Rwork | 0.220 |
R-free | 0.25180 * |
Structure solution method | COMBINED MAD AND MIRAS |
RMSD bond length | 0.006 |
RMSD bond angle | 1.170 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.350 |
High resolution limit [Å] | 2.310 | 2.310 |
Rmerge | 0.031 | 0.209 |
Total number of observations | 187531 * | |
Number of reflections | 55444 | |
<I/σ(I)> | 22.7 | 5.2 |
Completeness [%] | 99.2 | 99.6 |
Redundancy | 3.4 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 | 293 | Verboven, C.C., (1995) J. Steroid Biochem. Mol. Biol., 54, 11. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG400 | 7.5 (%(v/v)) | |
2 | 1 | reservoir | acetate | 0.1 (M) | pH4.6 |
3 | 1 | drop | protein | 30 (mg/ml) |