4MY2
Crystal Structure of Norrin in fusion with Maltose Binding Protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-10 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 59.458, 79.022, 104.241 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.400 |
| R-factor | 0.20816 |
| Rwork | 0.207 |
| R-free | 0.23740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c4m |
| RMSD bond length | 0.035 |
| RMSD bond angle | 1.643 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.156 | 0.883 |
| Number of reflections | 19865 | |
| <I/σ(I)> | 13.1 | 3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 9.5 | 9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 15% PEG 3350, 0.1 M sodium acetate, pH 4.6, 0.2 M ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
