5ICQ
Methanobactin periplasmic binding protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2015-10-12 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0332 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 122.200, 141.500, 83.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.003 - 1.900 |
| R-factor | 0.1584 |
| Rwork | 0.157 |
| R-free | 0.19450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3pam |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.824 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | BALBES |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.900 |
| Rmerge | 0.170 |
| Number of reflections | 56967 |
| <I/σ(I)> | 22.93 |
| Completeness [%] | 100.0 |
| Redundancy | 14.79 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | PEG3350, Bis-Tris, Lithium sulfate |
