2DVK
Crystal Structure of Hypothetical protein from Aeropyrum pernix
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-07-11 |
Detector | RIGAKU |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 55.870, 70.232, 91.579 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.460 - 1.800 |
R-factor | 0.234 |
Rwork | 0.234 |
R-free | 0.24900 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.066 | |
Number of reflections | 16254 | |
<I/σ(I)> | 16.2 | |
Completeness [%] | 97.0 | 97 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 295 | HEPES, PEG, pH 7.5, microbatch, temperature 295K |
1 | MICROBATCH | 7.5 | 295 | HEPES, PEG, pH 7.5, microbatch, temperature 295K |
1 | MICROBATCH | 7.5 | 295 | HEPES, PEG, pH 7.5, microbatch, temperature 295K |