2P6H
Crystal structure of hypothetical protein APE1520 from Aeropyrum pernix K1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-09-30 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 3 |
Unit cell lengths | 73.023, 73.023, 49.433 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.370 - 1.950 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.20300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vph |
RMSD bond length | 0.013 |
RMSD bond angle | 1.800 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.020 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.047 | 0.205 |
Number of reflections | 21386 | |
<I/σ(I)> | 26.1 | 15 |
Completeness [%] | 99.6 | 96.3 |
Redundancy | 5.3 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 291 | 0.1M HEPES, 1.5M Lithium Sulfate, pH7.5, MICROBATCH, temperature 291K |