3ZIE
SepF-like protein from Archaeoglobus fulgidus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-09-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9793, 0.9798 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 107.020, 64.090, 82.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.19073 |
Rwork | 0.188 |
R-free | 0.24416 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.025 |
RMSD bond angle | 2.055 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.000 | 2.110 |
High resolution limit [Å] | 1.960 | 2.000 |
Rmerge | 0.070 | 0.110 |
Number of reflections | 39136 | |
<I/σ(I)> | 29.9 | 22.8 |
Completeness [%] | 99.9 | 100 |
Redundancy | 14 | 14.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M LITHIUM SULFATE, 0.1 M SODIUM ACETATE PH 4.5, 30 %W/V PEG 8000 |