3IEF
Crystal structure of tRNA guanine-n1-methyltransferase from Bartonella henselae using MPCS.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 100 |
Collection date | 2009-06-19 |
Wavelength(s) | 0.97946 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.017, 84.467, 97.192 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
R-factor | 0.196 |
Rwork | 0.195 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1p9p |
RMSD bond length | 0.013 |
RMSD bond angle | 1.381 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.116 | 0.492 |
Number of reflections | 16569 | |
<I/σ(I)> | 18.2 | 3.8 |
Completeness [%] | 99.9 | 100 |
Redundancy | 8.9 | 8.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MPCS | 7 | 293 | Initial crystal hit JCSG+ condition G7 15% PEG 3350, 0.1M succinic acid pH 7.0 optimized with microcapillary gradient, MPCS, temperature 293K |