2E55
Structure of AQ2163 protein from Aquifex aeolicus
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 | 2006-10-04 |
Detector | RIGAKU |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 63.390, 70.670, 90.166 |
Unit cell angles | 90.00, 97.96, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.150 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.23000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1v9s |
RMSD bond length | 0.007 |
RMSD bond angle | 1.290 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.082 | 0.276 |
Number of reflections | 37617 | |
<I/σ(I)> | 7.7 | 3.1 |
Completeness [%] | 99.0 | 95 |
Redundancy | 3.8 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.6 | 295 | 32% PEG 4K, 0.1M LiSO4, 0.13M Tris-hydrochloride, pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 295K |