3V1D
Crystal structure of de novo designed MID1-cobalt
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 | 2011-04-26 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9494 |
Spacegroup name | P 1 |
Unit cell lengths | 27.720, 45.451, 62.112 |
Unit cell angles | 90.04, 90.00, 90.00 |
Refinement procedure
Resolution | 36.668 - 1.239 |
R-factor | 0.1474 |
Rwork | 0.147 |
R-free | 0.19410 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yzm |
RMSD bond length | 0.012 |
RMSD bond angle | 1.323 |
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] | 36.668 | 1.250 |
High resolution limit [Å] | 1.239 | 1.240 |
Rmerge | 0.068 | 0.429 |
Number of reflections | 81186 | |
<I/σ(I)> | 18.1 | 2 |
Completeness [%] | 94.3 | 82.6 |
Redundancy | 2.5 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 1-2 microliters protein (20 mg/ml, 100 mM ammonium acetate buffer) mixed with 1 microliter crystallization buffer (0.1 M MES pH 6.0, 30% PEG 200, 10% PEG 3000), VAPOR DIFFUSION, HANGING DROP, temperature 293K |