3DM0
Maltose Binding Protein fusion with RACK1 from A. thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-08-30 |
Detector | RIGAKU SATURN 92 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 57.777, 63.263, 70.056 |
Unit cell angles | 70.40, 88.38, 73.82 |
Refinement procedure
Resolution | 30.270 - 2.400 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.25000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hsj |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 34464 | |
<I/σ(I)> | 21.4 | 2.1 |
Completeness [%] | 98.8 | 95.5 |
Redundancy | 4.1 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 278 | 100mM HEPES pH 7.5 20% w/v PEG 10,000, VAPOR DIFFUSION, SITTING DROP, temperature 278K |