2O3A
Crystal structure of a protein AF_0751 from Archaeoglobus fulgidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 77 |
Detector technology | CCD |
Collection date | 2006-10-06 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.97958 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 53.294, 55.890, 108.784 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.035 - 2.200 |
R-factor | 0.233 |
Rwork | 0.230 |
R-free | 0.29200 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.439 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXD |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.490 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.109 | 0.504 |
Total number of observations | 19675 | |
Number of reflections | 16685 | |
<I/σ(I)> | 18 | 3.7 |
Completeness [%] | 97.7 | 91.3 |
Redundancy | 12.6 | 8.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 294 | 100mM Hepes pH 7.5, 30% MPD, 200mM tri-sodium citrate dihydrate, Vapor diffusion, temperature 294K |