1ZMG
Crystal structure of copper-bound engineered maltose binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 105 |
Detector technology | IMAGE PLATE |
Collection date | 2004-12-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 38.860, 43.950, 57.790 |
Unit cell angles | 101.46, 106.82, 102.60 |
Refinement procedure
Resolution | 38.120 - 2.500 |
R-factor | 0.233 |
Rwork | 0.211 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1omp |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.069 | 0.228 |
Number of reflections | 10811 | |
Completeness [%] | 96.6 | 95 |
Redundancy | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | PEG 2000 MME, copper sulphate, sodium acetate, Tris-HCl, sodium chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |