1TMY
CHEY FROM THERMOTOGA MARITIMA (APO-I)
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-01-19 |
| Detector | RIGAKU RAXIS II |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.040, 53.950, 34.160 |
| Unit cell angles | 90.00, 95.56, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.186 * |
| Rwork | 0.186 |
| Structure solution method | SIRAS / MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3chy |
| RMSD bond length | 0.017 |
| RMSD bond angle | 18.560 * |
| Data reduction software | R-AXIS |
| Data scaling software | R-AXIS |
| Phasing software | RSS |
| Refinement software | TNT (5E) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.250 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.053 | 0.120 |
| Number of reflections | 7985 | |
| <I/σ(I)> | 5.5 | 3 |
| Completeness [%] | 83.0 | 69 |
| Redundancy | 2.5 | 1.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS BUFFER (PH 8.5) AND 1.8M AMMONIUM PHOSPHATE |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | reservoir | Tris | 0.1 (M) | |
| 3 | 1 | reservoir | ammonium phosphate | 1.8 (M) |
