3FGT
Two chain form of the 66.3 kDa protein from mouse lacking the linker peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-10-31 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.80150 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 145.570, 88.220, 63.270 |
| Unit cell angles | 90.00, 98.10, 90.00 |
Refinement procedure
| Resolution | 29.488 - 2.400 |
| R-factor | 0.168 |
| Rwork | 0.166 |
| R-free | 0.20745 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fbx |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.493 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.488 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.096 | 0.459 |
| Total number of observations | 15401 | |
| Number of reflections | 31031 | |
| <I/σ(I)> | 9.5 | 3.5 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.4 | 3.4 |
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 |
