1EUF
BOVINE DUODENASE(NEW SERINE PROTEASE), CRYSTAL STRUCTURE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 295 |
Detector technology | IMAGE PLATE |
Collection date | 1997-08-04 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 64 |
Unit cell lengths | 100.117, 100.117, 39.753 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 99.000 - 2.400 |
Rwork | 0.179 |
R-free | 0.22300 |
RMSD bond length | 0.006 |
RMSD bond angle | 24.670 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 2.510 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.058 | 0.247 |
Total number of observations | 87183 * | |
Number of reflections | 8780 | |
<I/σ(I)> | 14.3 | |
Completeness [%] | 96.3 | 97.3 |
Redundancy | 9.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 4 * | Zamolodchikova, T.S., (1997) Eur. J. Biochem., 249, 612. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | PEG3350 | 10 (%) | |
3 | 1 | drop | K/Na phosphate | 50 (mM) | |
4 | 1 | drop | 1 (mM) | ||
5 | 1 | reservoir | PEG3350 | 14 (%sat) |