2B6H
Structure of human ADP-ribosylation factor 5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-09-14 |
| Detector | RIGAKU RAXIS IV |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 64.996, 81.640, 84.399 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.500 - 1.764 |
| Rwork | 0.201 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z6x |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.900 |
| High resolution limit [Å] | 1.760 | 3.010 | 1.760 |
| Rmerge | 0.068 | 0.035 | 0.306 |
| Number of reflections | 22373 | ||
| Completeness [%] | 98.8 | ||
| Redundancy | 5.9 | 6.1 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 277 | 25% PEG 4000, 0.2M ammonium sulfate, 0.1M sodium acetate, 3% 6-aminocaproic acid, pH 4.6, vapor diffusion, sitting drop, temperature 277K |
