3BUT
Crystal structure of protein Af_0446 from Archaeoglobus fulgidus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2007-12-13 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.97960 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 131.050, 28.330, 29.510 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.910 |
| R-factor | 0.22816 |
| Rwork | 0.226 |
| R-free | 0.29963 |
| Structure solution method | SAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.122 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.3.0034) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.142 | 0.630 |
| Number of reflections | 9264 | |
| <I/σ(I)> | 4.4 | 0.8 |
| Completeness [%] | 99.6 | 97.1 |
| Redundancy | 7.5 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 294 | 20% PEG 3350, 35mM Proline, 200mM Sodium formate, 10% Glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
