4HI2
Crystal structure of an Acylphosphatase protein cage
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | ENRAF-NONIUS FR591 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-07-13 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 |
Unit cell lengths | 104.940, 104.940, 147.811 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.178 - 3.100 |
R-factor | 0.2244 |
Rwork | 0.221 |
R-free | 0.28910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2bjd |
RMSD bond length | 0.009 |
RMSD bond angle | 1.340 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.180 | |
High resolution limit [Å] | 3.100 | 3.100 |
Number of reflections | 31972 | |
<I/σ(I)> | 5.8 | |
Completeness [%] | 96.8 | 96.8 |
Redundancy | 1.8 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 1.6M AMS, 0.1M HEPES, pH=7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |