2H9B
Crystal structure of the effector binding domain of a BenM variant (BenM R156H/T157S)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-BM |
| Synchrotron site | APS |
| Beamline | 22-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.510, 66.587, 117.971 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.700 - 1.800 |
| R-factor | 0.171 |
| Rwork | 0.168 |
| R-free | 0.21000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB accession code 2F97 BenM-EBD (high pH) |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.989 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.078 | 0.464 |
| Number of reflections | 48633 | 4763 |
| Completeness [%] | 100.0 | 99.77 |
| Redundancy | 6.9 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 296.4 | Precipitant:2.0 M ammonium sulfate Protein: 20 mM tris HCl, 0.5 M NaCl, pH 7.9, 10% glycerol Equal volumes mixed, Microbatch under oil, temperature 296.4K |
