Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ELLIOTT GX-21 |
| Temperature [K] | 293 |
| Detector technology | DIFFRACTOMETER |
| Collection date | 1992-06 |
| Detector | ENRAF-NONIUS FAST |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 120.887, 111.903, 65.748 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 |
| R-factor | 0.187 |
| Rwork | 0.182 |
| R-free | 0.23000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cdg |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.147 |
| Data reduction software | BIOMOL |
| Data scaling software | BIOMOL |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.000 | 2.580 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.086 | |
| Number of reflections | 59552 | |
| Completeness [%] | 73.9 | 40.3 |
| Redundancy | 2.42 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 5.5 * | PROTEIN WAS CRYSTALLIZED FROM OTHER LIQUOR CONTAINING 60% V/V METHYL-PENTANEDIOL (MPD) 100 MM SODIUM-HEPES PH 7.55 AND 0.5% W/V MALTOSE THEN SOAKED IN MOTHER LIQUOR WITH 0.1 % ACARBOSE AND 0.5 % MALTOSE FOR 5 DAYS |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 28.7 (mg/ml) | |
| 2 | 1 | drop | ammonium acetate | 50 (mM) | |
| 3 | 1 | drop | alpha-cyclodextrin | 50 (mg/ml) | |
| 4 | 1 | reservoir | MPD | 60 (%(v/v)) | |
| 5 | 1 | reservoir | sodium Hepes | 100 (mM) |
