3RWV
Crystal Structure of apo-form of Human Glycolipid Transfer Protein at 1.5 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9754 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 82.205, 82.205, 148.275 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 1.500 |
| R-factor | 0.14564 |
| Rwork | 0.144 |
| R-free | 0.17583 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.395 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.072 | 0.249 |
| Number of reflections | 76833 | |
| <I/σ(I)> | 15.6 | 4.6 |
| Completeness [%] | 99.3 | 98.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 273 | 15-20%PEG 8000, 0.1M MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 273K |
