1ES0
CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 96 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-01-16 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 95.149, 110.123, 96.084 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.960 - 2.600 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | I-A(K) - PDB CODE 1IAK |
| RMSD bond length | 0.006 |
| RMSD bond angle | 26.000 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((TRUNCATE)) |
| Phasing software | AMoRE |
| Refinement software | CNS (0.9) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.960 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.068 * | 0.353 * |
| Total number of observations | 66107 * | |
| Number of reflections | 15754 | |
| <I/σ(I)> | 15.7 | 4.2 |
| Completeness [%] | 99.3 | 99.6 |
| Redundancy | 4.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 * | 277 | seeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 10 (mg/ml) | |
| 2 | 1 | 1 | HEPES | 20 (mM) | |
| 3 | 1 | 1 | 25 (mM) |
