4QQG
Crystal structure of an N-terminal HTATIP fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-02-11 |
| Detector | adsc q315 |
| Wavelength(s) | 1.2830 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.544, 59.986, 101.638 |
| Unit cell angles | 90.00, 100.65, 90.00 |
Refinement procedure
| Resolution | 99.890 - 2.800 |
| R-factor | 0.2277 |
| Rwork | 0.226 |
| R-free | 0.25950 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2eko |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.384 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.3.6) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 42.260 | 42.260 | 2.950 |
| High resolution limit [Å] | 2.800 | 8.850 | 2.800 |
| Rmerge | 0.134 | 0.034 | 0.565 |
| Total number of observations | 1466 | 6923 | |
| Number of reflections | 12878 | ||
| <I/σ(I)> | 10.1 | 24 | 2.8 |
| Completeness [%] | 99.9 | 98.6 | 99.9 |
| Redundancy | 3.7 | 3.4 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 291 | 20% PEG3350, 0.2 M calcium acetate. The protein sample may have been treated with trypsin, VAPOR DIFFUSION, temperature 291K |
