1P9Q
Structure of a hypothetical protein AF0491 from Archaeoglobus fulgidus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-17 |
Detector | SBC-2 |
Spacegroup name | P 1 |
Unit cell lengths | 33.875, 44.254, 61.418 |
Unit cell angles | 92.74, 118.02, 109.67 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.219 |
R-free | 0.27000 |
Structure solution method | MAD |
Starting model (for MR) | None |
RMSD bond length | 0.019 |
RMSD bond angle | 1.600 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SnB (+ PHASES + SHARP) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 35721 | |
<I/σ(I)> | 23.2 | 3.8 |
Completeness [%] | 92.2 | 84.6 |
Redundancy | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 294 | Sodium acetate, PEG 3350, Ethylene Glycole, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 294K, pH 7.80 |