3CAZ
Crystal structure of a BAR protein from Galdieria sulphuraria
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 | 2007-08-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.96411 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 78.962, 78.962, 456.028 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.168 - 3.344 |
| R-factor | 0.217 |
| Rwork | 0.215 |
| R-free | 0.25200 |
| Structure solution method | SAD |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.904 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 47.168 | 47.168 | 3.470 |
| High resolution limit [Å] | 3.344 | 7.220 | 3.344 |
| Rmerge | 0.085 | 0.046 | 0.858 |
| Number of reflections | 13119 | ||
| <I/σ(I)> | 11.425 | 1.622 | |
| Completeness [%] | 98.3 | 94.1 | 98.2 |
| Redundancy | 12.8 | 11.8 | 9.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | Protein solution (10 mg/mL Se-Met protein, 0.05 M Sodium chloride, 0.0003 M TCEP, 0.005 M Bis-Tris pH 7.0) mixed in a 1:1 ratio with the Well solution (27% MPD, 0.12 M Magnesium chloride, 0.1 M MES/Acetate pH 5.5), VAPOR DIFFUSION, HANGING DROP, temperature 277K |






