3Q1Y
Allosteric regulation by Lysine residue: A novel anion-hole formation in the ribokinase family
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 88.912, 44.717, 87.955 |
| Unit cell angles | 90.00, 113.48, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.030 |
| R-factor | 0.1899 |
| Rwork | 0.188 |
| R-free | 0.22810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hic |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.088 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Number of reflections | 20195 | |
| <I/σ(I)> | 6.7 | 10.1 |
| Completeness [%] | 99.2 | 94 |
| Redundancy | 13.7 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 292 | 0.2M MgCl2,200mMCsCl, 20% PEG 3350 0.1M Bis-Tris pH 6.5), VAPOR DIFFUSION, SITTING DROP, temperature 292K |
