1NE7
HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE
Replaces: 1D9TExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 93 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-03-18 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.78 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 109.877, 110.892, 180.881 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.970 - 1.750 |
| R-factor | 0.1954 |
| Rwork | 0.193 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dea |
| RMSD bond length | 0.005 |
| RMSD bond angle | 23.100 * |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.970 | 1.860 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.052 * | 0.224 * |
| Number of reflections | 209143 | |
| <I/σ(I)> | 9.9 | 3.4 |
| Completeness [%] | 94.3 | 96.8 * |
| Redundancy | 3.8 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 18 * | 1.68 M ammonium sulphate, 10 mM N-acetyl-glucosamine-6-phosphate and 0.1 mM 2-deoxy-2-amino D-glucitol 6-phosphate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.68 (M) | |
| 3 | 1 | reservoir | N-acetyl-glucosamine-6-phosphate | 10 (mM) | |
| 4 | 1 | reservoir | 2-deoxy-2-amino-D-glucitol-6-phosphate | 0.1 (mM) | pH7. |
