1NUC
STAPHYLOCOCCAL NUCLEASE, V23C VARIANT
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 278.15 |
Detector technology | IMAGE PLATE |
Collection date | 1996-01 |
Detector | MACSCIENCE |
Spacegroup name | P 41 |
Unit cell lengths | 47.400, 47.400, 62.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 1.900 |
R-factor | 0.173 |
Rwork | 0.173 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1snc |
RMSD bond length | 0.010 |
RMSD bond angle | 24.719 * |
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] | 6.000 | 1.980 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.069 | 0.072 |
Number of reflections | 9359 | |
<I/σ(I)> | 10 | 3 |
Completeness [%] | 87.9 | 76.5 |
Redundancy | 3.7 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8.15 | 4 * | Loll, P.J., (1989) Proteins Struct. Funct. Genet., 5, 183. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 10.5 (mM) | |
3 | 1 | drop | MPD | 17 (%(w/w)) | |
4 | 1 | drop | 10 (mM) | ||
5 | 1 | drop | potassium citrate | 20 (mM) | |
6 | 1 | reservoir | potassium phosphate | 10.5 (mM) | |
7 | 1 | reservoir | MPD | 21-23 (%(w/w)) |