2B3M
Crystal structure of protein AF1124 from Archaeoglobus fulgidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-06-21 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97942 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 57.596, 57.596, 142.993 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.850 |
R-factor | 0.17891 |
Rwork | 0.177 |
R-free | 0.20534 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.401 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.104 | 0.489 |
Number of reflections | 39149 | |
<I/σ(I)> | 47.8 | 3.9 |
Completeness [%] | 99.6 | 96.7 |
Redundancy | 14.1 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | Ammonium Citrate, Bis-Tris propane, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |