3RFI
Crystal structure of the saposin-like domain of plant aspartic protease from Solanum tuberosum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | OTHER |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-11-09 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 56.470, 56.470, 55.340 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.900 |
R-factor | 0.18995 |
Rwork | 0.187 |
R-free | 0.24980 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 1.808 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.059 | 0.900 |
Number of reflections | 8355 | |
<I/σ(I)> | 24.1 | 2.87 |
Completeness [%] | 99.9 | 100 |
Redundancy | 10.3 | 10.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2M Lithium sulfate monohydrate, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |