5TQB
Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with ribosomal protein L4 (RpL4)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-03-28 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 121.000, 127.900, 42.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.949 - 2.400 |
R-factor | 0.1909 |
Rwork | 0.189 |
R-free | 0.22470 |
Structure solution method | SAD |
RMSD bond length | 0.004 |
RMSD bond angle | 0.735 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SHARP |
Refinement software | PHENIX (1.8.2_1309) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.540 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 49797 | 8039 |
<I/σ(I)> | 13.6 | 1.92 |
Completeness [%] | 99.1 | 99.1 |
Redundancy | 6.8 | 6.6 |
CC(1/2) | 0.990 | 0.900 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 294 | 0.1 M BIS-TRIS (pH 5.5) 2 % (v/v) Tacsminate (pH 5.5) 13 % (w/v) PEG 3350 |