1N3W
Engineered High-Affinity Maltose-Binding Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-12-07 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54179 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 121.510, 121.510, 61.380 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.400 * - 2.600 |
R-factor | 0.244 |
Rwork | 0.244 |
R-free | 0.28600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf |
RMSD bond length | 0.007 * |
RMSD bond angle | 22.700 * |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 27.390 | 2.690 |
High resolution limit [Å] | 2.600 | 2.590 |
Rmerge | 0.065 | 0.196 * |
Number of reflections | 16214 | |
<I/σ(I)> | 30.1 | |
Completeness [%] | 99.8 * | 99.9 * |
Redundancy | 4.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 290 | PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | cacodylate | 10 (mM) | pH6.5 |
2 | 1 | reservoir | 200 (mM) | ||
3 | 1 | reservoir | zinc acetate | 18 (mM) | |
4 | 1 | reservoir | PEG8000 | 20 (%) |