2HT1
The closed ring structure of the Rho transcription termination factor in complex with nucleic acid in the motor domains
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Wavelength(s) | 1.1 |
| Spacegroup name | I 4 3 2 |
| Unit cell lengths | 257.686, 257.686, 257.686 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 3.510 |
| R-factor | 0.28707 |
| Rwork | 0.294 |
| R-free | 0.32810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pvo |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.950 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.680 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Number of reflections | 15818 | |
| Completeness [%] | 92.0 | 86.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microbatch under paraffine oil | 6.5 | 291 | 50 mM Na cacodylate, 10 mM MgOAc, 1.8 M LiSO4, 2% benzamidine, 10 mM spermine-HCl, pH 6.5, Microbatch under paraffine oil, temperature 291K |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | Na cacodylate | ||
| 10 | 1 | 2 | HOH | ||
| 2 | 1 | 1 | MgOAc | ||
| 3 | 1 | 1 | LiSO4 | ||
| 4 | 1 | 1 | benzamidine | ||
| 5 | 1 | 1 | spermine-HCl | ||
| 6 | 1 | 1 | HOH | ||
| 7 | 1 | 2 | Na cacodylate | ||
| 8 | 1 | 2 | MgOAc | ||
| 9 | 1 | 2 | LiSO4 |
