6K67
Application of anti-helix antibodies in protein structure determination (9011-3LRH)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 7A (6B, 6C1) |
| Synchrotron site | PAL/PLS |
| Beamline | 7A (6B, 6C1) |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2016-07-19 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | H 3 |
| Unit cell lengths | 115.298, 115.298, 93.275 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.380 - 1.950 |
| R-factor | 0.20441 |
| Rwork | 0.203 |
| R-free | 0.23650 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3lrh 2w73 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.505 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rpim | 0.043 | 0.260 |
| Number of reflections | 33481 | 3373 |
| <I/σ(I)> | 27.3 | |
| Completeness [%] | 99.7 | |
| Redundancy | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 296 | 50% PEG 400, 0.2M CaCl2, 0.1M HEPES pH 7.5 |
