3V1E
Crystal structure of de novo designed MID1-zinc H12E mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-12 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 27.052, 47.212, 55.352 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.920 - 1.073 |
R-factor | 0.1464 |
Rwork | 0.145 |
R-free | 0.15910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yzm |
RMSD bond length | 0.009 |
RMSD bond angle | 1.316 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.3_927)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.920 | 1.080 |
High resolution limit [Å] | 1.073 | 1.070 |
Rmerge | 0.130 | 0.383 |
Number of reflections | 58547 | |
<I/σ(I)> | 20.3 | 2.1 |
Completeness [%] | 97.6 | 87.2 |
Redundancy | 3.7 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | 1-2 microliters protein (20 mg/ml, 100 mM ammonium acetate buffer) mixed with 1 microliter crystallization buffer (0.1 M bicine pH 9.0, 27% PEG 3350), VAPOR DIFFUSION, HANGING DROP, temperature 293K |