3LIA
Crystal Structure of the extracellular domain of the putative histidine kinase mmHK1S-Z2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-02-02 |
| Wavelength(s) | 0.97157 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.525, 98.494, 71.040 |
| Unit cell angles | 90.00, 87.51, 90.00 |
Refinement procedure
| Resolution | 40.464 - 1.990 |
| R-factor | 0.182 |
| Rwork | 0.178 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.024 |
| RMSD bond angle | 1.958 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (1.3.1) |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
| Rmerge | 0.065 | 0.036 | 0.251 |
| Number of reflections | 43582 | ||
| <I/σ(I)> | 14.8 | ||
| Completeness [%] | 99.8 | 99.7 | 98.5 |
| Redundancy | 4.2 | 4.1 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 5.6 | 293 | 15% PEG3350, 0.21M NH4SO4, 0.1M bistris, pH 5.6, vapor diffusion, temperature 293K |
