8OLJ
Crystal structure of Archaeoglobus fulgidus AfAgo-N protein representing N-L1-L2 domains
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1) |
Synchrotron site | PETRA III, EMBL c/o DESY |
Beamline | P13 (MX1) |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-11-23 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 0.97970 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 75.264, 75.264, 94.722 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 53.700 - 1.400 |
R-factor | 0.1479 |
Rwork | 0.145 |
R-free | 0.17772 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.610 |
Data reduction software | XDS (VERSION Jan 26, 2018 BUILT=20180126) |
Data scaling software | Aimless (version 0.7.2) |
Phasing software | MOLREP (Vers 11.6.04) |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 94.720 | 1.420 |
High resolution limit [Å] | 1.400 | 1.400 |
Rmerge | 0.047 | 0.908 |
Rmeas | 0.049 | 0.967 |
Rpim | 0.016 | 0.331 |
Number of reflections | 61624 | 3045 |
<I/σ(I)> | 23.8 | 2.3 |
Completeness [%] | 100.0 | 100 |
Redundancy | 9.7 | 8.4 |
CC(1/2) | 0.999 | 0.810 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 280 | Protein concentration 4.1 mg/ml. Reservoir: TrisHCl pH 8.0 0.05 M; iPrOH 27%; ammonium acetate 0.11 M; Bicine pH 9.0 0.05 M. Cryo-protection: short wash in 0.16 M Ammonium acetate; 0.08 M TrisHCl pH 8.5; 24% iPrOH; Glycerol 20% |