2EGI
Crystal Structure of a Hypothetical Protein(AQ1494) from Aquifex aeolicus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B2 |
Synchrotron site | SPring-8 |
Beamline | BL26B2 |
Temperature [K] | 180 |
Detector technology | CCD |
Collection date | 2006-11-13 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 0.97884,0.9000,0.97973 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 98.493, 97.754, 113.194 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.720 - 2.300 |
R-factor | 0.24 |
Rwork | 0.240 |
R-free | 0.28200 |
Structure solution method | MAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.200 |
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 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.085 | 0.416 |
Number of reflections | 74399 | |
Completeness [%] | 99.6 | 98.8 |
Redundancy | 6.8 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.5 | 293 | 20% PEG8000, 0.1M HEPES pH7.5, micro batch, temperature 293K |