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 |