3VMF
Archaeal protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32XU |
| Synchrotron site | SPring-8 |
| Beamline | BL32XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-12 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 176.567, 55.169, 90.689 |
| Unit cell angles | 90.00, 101.61, 90.00 |
Refinement procedure
| Resolution | 46.498 - 2.300 |
| R-factor | 0.2042 |
| Rwork | 0.201 |
| R-free | 0.26060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3AGJ 3agk |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.202 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.7.2_869)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Number of reflections | 38192 | |
| <I/σ(I)> | 37.7 | 3.82 |
| Completeness [%] | 98.9 | 97.2 |
| Redundancy | 5.7 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 23% PEG 3350, 200mM Ammonium sulfate, 10mM L-proline, 100mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
