2OO2
Crystal structure of protein AF1782 from Archaeoglobus fulgidus, Pfam DUF357
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-01-20 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97958 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 44.631, 46.452, 43.177 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.242 |
Rwork | 0.240 |
R-free | 0.28900 |
Structure solution method | SAD |
RMSD bond length | 0.029 |
RMSD bond angle | 1.954 |
Data reduction software | HKL-2000 |
Data scaling software | SCALA |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.193 | 1.890 |
High resolution limit [Å] | 1.795 | 1.795 |
Rmerge | 0.080 | 0.549 |
Total number of observations | 7358 | |
Number of reflections | 8690 | |
<I/σ(I)> | 20.6 | 2.4 |
Completeness [%] | 98.5 | 91.8 |
Redundancy | 8.9 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 294 | 100mM Tris-HCl pH 7.5, 3.2M 1,6-hexanediol, 200mM Magnesium chloride, VAPOR DIFFUSION, temperature 294K |