3B7X
Crystal structure of human FK506-Binding Protein 6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-09-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | I 41 2 2 |
| Unit cell lengths | 55.059, 55.059, 229.965 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.100 |
| R-factor | 0.2577 |
| Rwork | 0.256 |
| R-free | 0.28215 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kt0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.489 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Number of reflections | 10831 | |
| <I/σ(I)> | 46.3 | 6.7 |
| Completeness [%] | 99.2 | 97.6 |
| Redundancy | 9.1 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | Mixed equal volumes of 1.6M MgSO4, 0.1M MES pH 6.5, and 10 mg/mL protein. Crystals were cryoprotected by transferring the crystals to a drop containing mother liquor to which glycerol was added to a final concentration of 20%, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
