3SEV
Zn-mediated Trimer of Maltose-binding Protein E310H/K314H by Synthetic Symmetrization
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) | 0.9795 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 113.780, 115.720, 119.450 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.060 - 3.050 |
R-factor | 0.2229 |
Rwork | 0.221 |
R-free | 0.26300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.100 |
Data scaling software | XSCALE |
Phasing software | PHASER (2.1.4) |
Refinement software | BUSTER-TNT |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 39.060 | 3.130 | |
High resolution limit [Å] | 3.050 | 13.640 | 3.050 |
Rmerge | 0.123 | 0.034 | 0.543 |
Number of reflections | 30645 | 379 | 2231 |
<I/σ(I)> | 10.39 | 24.86 | 2.43 |
Completeness [%] | 99.6 | 91.1 | 99.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 290 | 0.1M HEPES, 2.4M AMMONIUM SULFATE, pH 8.0, vapor diffusion, hanging drop, temperature 290K |