1UOY
The bubble protein from Penicillium brevicompactum Dierckx exudate.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 2002-01-15 |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 43.615, 58.436, 53.415 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 * - 1.500 |
R-factor | 0.164 |
Rwork | 0.164 |
R-free | 0.18500 |
Structure solution method | SAD |
RMSD bond length | 0.013 |
RMSD bond angle | 25.500 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELXD |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 * | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.055 | 0.155 |
Total number of observations | 151997 * | |
Number of reflections | 11250 | |
<I/σ(I)> | 8.3 | 3.6 |
Completeness [%] | 99.9 | 99.9 * |
Redundancy | 13.5 | 12.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5 | 277 | 16 MG/ML PROTEIN IN 30 MM NA-ACETATE BUFFER, PH 5.0 AT 4 DEG. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 14 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 17 (%(w/v)) |