3FGW
One chain form of the 66.3 kDa protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-05 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 1.8 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 146.690, 88.110, 73.550 |
| Unit cell angles | 90.00, 111.10, 90.00 |
Refinement procedure
| Resolution | 46.070 - 2.800 |
| R-factor | 0.22423 |
| Rwork | 0.223 |
| R-free | 0.24921 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fbx |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.983 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.070 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.139 | 0.430 |
| Number of reflections | 21117 | |
| <I/σ(I)> | 5.6 | 2 |
| Completeness [%] | 97.2 | 96.2 |
| Redundancy | 3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 12% (w/v) PEG 4000, 100mM NH4Ac, 100mM NaAc/HAc pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
