5FFT
Crystal Structure of Surfactant Protein-A Y221A Mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-07-06 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 63 |
Unit cell lengths | 97.125, 97.125, 44.576 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 14.308 - 2.200 |
R-factor | 0.1728 |
Rwork | 0.169 |
R-free | 0.20700 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.714 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 90.000 | 90.000 | 2.070 |
High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
Rmerge | 0.062 | 0.036 | 0.747 |
Total number of observations | 75389 | ||
Number of reflections | 16339 | ||
<I/σ(I)> | 18.7 | ||
Completeness [%] | 99.2 | 94.8 | 99.1 |
Redundancy | 4.6 | 4.6 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 290 | Crystals were grown in hanging drops over reservoirs containing 10 mM sodium cacodylate (pH 6.0), 10 mM calcium acetate, and 10% (w/v) PEG 20,000 |