1FMT
METHIONYL-TRNAFMET FORMYLTRANSFERASE FROM ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 193 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-07-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 151.040, 151.040, 81.800 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 8.000 - 2.000 |
| R-factor | 0.214 |
| Rwork | 0.214 |
| R-free | 0.25600 |
| Structure solution method | MIR |
| RMSD bond length | 0.011 |
| RMSD bond angle | 23.700 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.000 | 2.040 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.054 * | |
| Number of reflections | 71246 | |
| <I/σ(I)> | 8 | 2.7 |
| Completeness [%] | 96.6 | 77.7 |
| Redundancy | 3.2 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.3 | 6 * | Schmitt, E., (1996) Proteins. Struct.Funct. Genet., 25, 139. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | ammonium salfate | 45-52 (%) | |
| 2 | 1 | drop | potassium phosphate | 10 (mM) | |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | 2-mercaptoethanol | 10 (mM) | |
| 5 | 1 | drop | glycerol | 2-10 (%) | |
| 6 | 1 | drop | protein | 10-20 (mg/ml) |
