2AU3
Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase 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 |
| Detector technology | CCD |
| Collection date | 2003-12-01 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.222, 66.403, 138.157 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.000 |
| R-factor | 0.20488 |
| Rwork | 0.203 |
| R-free | 0.23826 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Low-resolution Aquifex aeolicus DnaG from Tm-soak MAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.223 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 25989 | |
| <I/σ(I)> | 14.3 | 3.3 |
| Completeness [%] | 99.0 | 93.8 |
| Redundancy | 3.45 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 7.5 | 291 | 18-22% EtOH, 55 mM HEPES, 100 mM NaCl, pH 7.5, Microbatch, temperature 291K |
