3LHR
Crystal structure of the SCAN domain from Human ZNF24
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-08-24 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.055, 50.029, 91.301 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 33.730 - 1.900 |
| R-factor | 0.184 |
| Rwork | 0.182 |
| R-free | 0.24300 |
| Structure solution method | SAD |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.861 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.082 | 0.456 |
| Number of reflections | 15875 | |
| <I/σ(I)> | 12.3 | |
| Completeness [%] | 97.3 | 76.5 |
| Redundancy | 13.3 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | Protein solution at 1.5 mM concentration was mixed 1:1 with a reservoir solution composed of 100 mM HEPES buffer, pH 7.5, 40 mM MgCl2, 24% MEPEG 2000, 2 mM thimerosal. Crystals were cryoprotected with reservoir solution supplemented with 10% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 291K |






