3FGR
Two chain form of the 66.3 kDa protein at 1.8 Angstroem
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-07 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.91841 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 148.737, 89.560, 64.811 |
| Unit cell angles | 90.00, 98.69, 90.00 |
Refinement procedure
| Resolution | 29.260 - 1.800 |
| R-factor | 0.15314 |
| Rwork | 0.152 |
| R-free | 0.18163 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fbx |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.533 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.033 | 0.419 |
| Number of reflections | 91683 | |
| <I/σ(I)> | 32.075 | |
| Completeness [%] | 99.5 | 96.2 |
| Redundancy | 3.2 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 12% (w/v) PEG 4000, 200mM NH4AC, 100mM NaAc/HAc pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
