3IRA
The crystal structure of one domain of the conserved protein from Methanosarcina mazei Go1
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9794, 0.9796 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 63.843, 63.843, 95.859 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 53.150 - 2.100 |
R-factor | 0.18849 |
Rwork | 0.187 |
R-free | 0.21783 |
Structure solution method | MAD |
RMSD bond length | 0.021 |
RMSD bond angle | 1.800 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.5.0054) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 53.150 | 2.154 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.112 | 0.630 |
Number of reflections | 11532 | |
<I/σ(I)> | 35.92 | 1.93 |
Completeness [%] | 99.8 | 100 |
Redundancy | 17.8 | 10.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | 0.2M ammonium acetate, 0.1M HEPES, 25% PEG3350, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |