4Z2A
Crystal structure of unglycosylated apo human furin @1.89A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-08-10 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.54 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 95.983, 66.597, 88.443 |
Unit cell angles | 90.00, 122.41, 90.00 |
Refinement procedure
Resolution | 29.581 - 1.890 |
R-factor | 0.149 |
Rwork | 0.148 |
R-free | 0.18340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p8j |
RMSD bond length | 0.010 |
RMSD bond angle | 1.260 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.960 |
High resolution limit [Å] | 1.890 | 4.070 | 1.890 |
Rmerge | 0.049 | 0.027 | 0.148 |
Total number of observations | 135597 | ||
Number of reflections | 37707 | ||
<I/σ(I)> | 13.7 | ||
Completeness [%] | 99.8 | 99.7 | 98.8 |
Redundancy | 3.6 | 3.7 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | Well 13% PEG 8K, 0.110M K-dihydrogen phosphate, 0.1M HEPES pH 7.5, 350 uL protein with 350uL well drops, MRC sitting drop |