4QT6
Crystal structure of the SPRY domain of human HERC1
Experimental procedure
Experimental method | SAD |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E SUPERBRIGHT |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-06-26 |
Detector | RIGAKU SATURN A200 |
Wavelength(s) | 1.5406 |
Spacegroup name | I 2 3 |
Unit cell lengths | 99.730, 99.730, 99.730 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.640 |
R-factor | 0.1711 |
Rwork | 0.170 |
R-free | 0.21230 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.433 |
Data reduction software | HKL-3000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE (2 .13) |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.670 |
High resolution limit [Å] | 1.640 | 4.450 | 1.640 |
Rmerge | 0.056 | 0.029 | 0.864 |
Number of reflections | 20404 | ||
<I/σ(I)> | 80.4 | ||
Completeness [%] | 99.9 | 98.6 | 100 |
Redundancy | 27.8 | 25.6 | 27.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.5 uL protein (mixed 1:700 w/w chymotrypsin:protein before setup) + 0.5 uL well solution (16% w/v PEG 8000, 0.04 M potassium phosphate monobasic, 20% v/v glycerol) + 0.1 uL 40% formamide (4% final concentration), VAPOR DIFFUSION, SITTING DROP, temperature 293K |