3LHD
Crystal structure of P. abyssi tRNA m1A58 methyltransferase in complex with S-adenosyl-L-homocysteine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-09-02 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.030, 127.577, 151.396 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.780 - 2.590 |
| R-factor | 0.23335 |
| Rwork | 0.231 |
| R-free | 0.28614 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1i9g |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.221 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.100 | 2.730 |
| High resolution limit [Å] | 2.590 | 2.590 |
| Rmerge | 0.046 | 0.197 |
| Number of reflections | 38327 | |
| <I/σ(I)> | 11.7 | 2.4 |
| Completeness [%] | 94.4 | 68.6 |
| Redundancy | 5.4 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 0.2M ammonium sulfate, 0.1M sodium acetate, 25% PEG 4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
