3RPF
Protein-protein complex of subunit 1 and 2 of Molybdopterin-converting factor from Helicobacter pylori 26695
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-20 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | F 2 2 2 |
Unit cell lengths | 88.187, 127.582, 187.945 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.000 - 1.900 |
R-factor | 0.204 |
Rwork | 0.202 |
R-free | 0.24200 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 0.985 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((phenix.refine: 1.7_650)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.082 | |
Number of reflections | 41239 | |
<I/σ(I)> | 25 | |
Completeness [%] | 99.1 | 99.8 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 277 | 0.2 M Ammonium sulfate 25% Peg 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |