2VP3
DC26 MUTANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE AND M7G(5')PPPG
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 103 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-05-30 |
| Detector | MACSCIENCE |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 84.600, 67.300, 79.600 |
| Unit cell angles | 90.00, 117.30, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.950 |
| R-factor | 0.224 |
| Rwork | 0.224 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vpt |
| RMSD bond length | 0.030 |
| RMSD bond angle | 2.700 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.049 | 0.310 |
| Number of reflections | 28824 | |
| <I/σ(I)> | 35 | 4 |
| Completeness [%] | 99.3 | 96 |
| Redundancy | 4 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | other * | 4.5 * | macro-seeding, Hodel, A.E., (1996) Cell(Cambridge,Mass.), 85, 247. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | PEG8000 | 10 (%) | |
| 2 | 1 | 1 | 0.125 (M) | ||
| 3 | 1 | 1 | citrate | 0.1 (M) |
