2H99
Crystal structure of the effector binding domain of a BenM variant (R156H,T157S)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 64.937, 66.506, 117.495 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.000 - 1.850 |
| R-factor | 0.167 |
| Rwork | 0.165 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB accession code 2F97 BenM-EBD (high pH) |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.085 |
| 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 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.073 | 0.484 |
| Number of reflections | 44035 | 4281 |
| <I/σ(I)> | 9.1 | |
| Completeness [%] | 99.7 | 99.3 |
| Redundancy | 5.1 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | microbatch under oil | 288.2 | Precipitant: 0.015 M magnesium acetate, 0.05 M sodium cacodlylate, 1.7 M ammonium sulfate Protein: 20 mM tris HCl, 0.5 M NaCl, pH 7.9, 10% glycerol Equal volumes mixed, microbatch under oil. The growing crystallization solution was in pH 6 and the protein solution was in pH 7.9 condition, temperature 288.2K |
