1N3X
Ligand-free 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 | 2001-09-30 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.5479 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.590, 71.330, 59.010 |
| Unit cell angles | 90.00, 101.53, 90.00 |
Refinement procedure
| Resolution | 23.800 * - 2.500 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.23400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1omp |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.000 * |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.790 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.480 |
| Rmerge | 0.083 | 0.174 |
| Number of reflections | 12399 * | |
| <I/σ(I)> | 21 | 9.5 |
| Completeness [%] | 98.0 * | 97.8 |
| Redundancy | 7.6 * |
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 | PEG4000 | 24 (%) | |
| 5 | 1 | reservoir | maltose | 1 (mM) |
