1LAX
CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOSE-BINDING PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2000-06-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.931 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.043, 89.115, 95.975 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.000 - 1.850 |
| R-factor | 0.15947 |
| Rwork | 0.157 |
| R-free | 0.20200 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1anf |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.423 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.058 | 0.201 |
| Number of reflections | 60245 | 8670 * |
| <I/σ(I)> | 9.2 | 3.4 |
| Completeness [%] | 99.8 | 99.2 |
| Redundancy | 7.5 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 17 * | PEG 4000, TRIS/HCl, ISOPROPANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5 |
| 2 | 1 | reservoir | isopropanol | 10 (%) | |
| 3 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
| 4 | 1 | drop | protein | 3.5 (mg/ml) |
