3SET
Ni-mediated Dimer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization (Form I)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-16 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9792 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 72.940, 62.270, 89.710 |
Unit cell angles | 90.00, 109.03, 90.00 |
Refinement procedure
Resolution | 42.896 - 1.900 |
R-factor | 0.234 |
Rwork | 0.232 |
R-free | 0.28220 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.805 |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 42.896 | 1.950 | |
High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
Rmerge | 0.139 | 0.048 | 0.501 |
Number of reflections | 60000 | 718 | 4416 |
<I/σ(I)> | 7.11 | 13.17 | 2.67 |
Completeness [%] | 99.6 | 97 | 99.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 290 | 0.1M TRIS, 25% (W/V) PEG 3350, pH 8.0, vapor diffusion, hanging drop, temperature 290K |