1ECR
ESCHERICHIA COLI REPLICATION TERMINATOR PROTEIN (TUS) COMPLEXED WITH DNA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 288 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-12-13 |
| Detector | FUJI |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 68.150, 68.150, 230.720 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.700 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.31400 |
| Structure solution method | MIR AND ANOMALOUS SCATTERING |
| Data reduction software | MACDENZO |
| Data scaling software | MACDENZO |
| Phasing software | CCP4 |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.060 * | |
| Number of reflections | 14018 | |
| Completeness [%] | 90.4 | 75.1 |
| Redundancy | 3.3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICRODIALYSIS | 5.3 | 293 | Kamada, K., (1996) Proteins: Struct.,Funct., Genet., 24, 402. * |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | WATER | ||
| 10 | 1 | 2 | DTT | ||
| 2 | 1 | 1 | PEG 4000 | ||
| 3 | 1 | 2 | WATER | ||
| 4 | 1 | 2 | PEG 4000 | ||
| 5 | 1 | 2 | NA CITRATE | ||
| 6 | 1 | 2 | NACL | ||
| 7 | 1 | 2 | GLYCEROL | ||
| 8 | 1 | 2 | SPERMINE | ||
| 9 | 1 | 2 | EDTA |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | protein | 0.25 (mM) | ||
| 2 | 1 | DNA duplex | 0.35 (mM) | ||
| 3 | 1 | Na citrate | 50 (mM) | ||
| 5 | 1 | glycerol | 10 (%(v/v)) | ||
| 6 | 1 | spermine | 2 (mM) | ||
| 7 | 1 | EDTA | 1 (mM) | ||
| 8 | 1 | DTT | 1 (mM) | ||
| 9 | 1 | PEG4000 | 10 (%(w/v)) |
