1NL5
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 | 2002-08-01 |
Detector | MARRESEARCH |
Wavelength(s) | 1.54179 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 121.590, 121.590, 62.440 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 60.800 - 2.100 |
R-factor | 0.252 |
Rwork | 0.252 |
R-free | 0.29000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf |
RMSD bond length | 0.006 |
RMSD bond angle | 22.100 * |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.800 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.046 * | 0.190 |
Completeness [%] | 99.9 | 100 |
Redundancy | 7.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.2 * | PEG 3350, Zinc Chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 100K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG5000 MME | 18-24 (%) | |
2 | 1 | reservoir | cacodylate | 0.1 (M) | pH6.2 |
3 | 1 | reservoir | sodium acetate | 200 (mM) | |
4 | 1 | reservoir | zinc acetate | 10 (mM) | |
5 | 1 | reservoir | 5 (mM) | ||
6 | 1 | reservoir | maltose | 1 (mM) |