1JEO
Crystal Structure of the Hypothetical Protein MJ1247 from Methanococcus jannaschii at 2.0 A Resolution Infers a Molecular Function of 3-Hexulose-6-Phosphate isomerase.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 280 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-09-15 |
| Detector | RIGAKU RAXIS II |
| Wavelength(s) | 1.5418 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 67.921, 68.155, 83.336 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.1891 * |
| Rwork | 0.189 |
| R-free | 0.22650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MJ1247 model obtained from MAD data (selenomethionine-derivatized crystals) |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.393 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.080 * | 0.320 |
| Total number of observations | 37198 * | |
| Number of reflections | 12655 * | |
| <I/σ(I)> | 11.5 | 1.98 |
| Completeness [%] | 94.0 * | 75.5 * |
| Redundancy | 4.44 | 1.63 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 22 * | 40% PEG 400, 0.1 M Tris/HCl, 0.2 M Sodium citrate, 10 mM betamercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG400 | 40 (%) | |
| 2 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8.5 |
| 3 | 1 | reservoir | sodium citrate | 0.2 (M) | |
| 4 | 1 | reservoir | beta-mercaptoethanol | 10 (mM) |
