6UKO
Structure analysis of full-length mouse bcs1 complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-04-23 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.00 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 254.055, 161.127, 132.595 |
Unit cell angles | 90.00, 107.27, 90.00 |
Refinement procedure
Resolution | 24.910 - 4.400 |
R-factor | 0.3584 |
Rwork | 0.357 |
R-free | 0.40670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | cryoEM |
RMSD bond length | 0.004 |
RMSD bond angle | 0.798 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.17_3644) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 4.560 |
High resolution limit [Å] | 4.400 | 4.400 |
Rmerge | 0.078 | |
Rpim | 0.034 | |
Number of reflections | 32257 | 3169 |
<I/σ(I)> | 19.09 | 1.38 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.2 | 5.6 |
CC(1/2) | 0.306 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 277 | Protein was premixed with 2mM ATP-gamma-S and 20 mM MgCl2 incubated for 30 min on ice, then centrifuged and the supernatant was mixed with 100 mM Tris pH 9.0, 100 mM NaCl, 60 mM MgCl2, 15% PEG400 |