1VP3
VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 1996-04-12 |
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 - 1.900 |
R-factor | 0.215 |
Rwork | 0.215 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vpt |
RMSD bond length | 0.010 |
RMSD bond angle | 1.800 |
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 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.057 | 0.210 |
Number of reflections | 24966 | |
<I/σ(I)> | 18.2 | 2.2 |
Completeness [%] | 79.0 | 27 |
Redundancy | 3 | 1 |
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) |