1J71
Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | SIEMENS |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1994-06-27 |
Detector | SIEMENS-NICOLET X100 |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.960, 51.430, 128.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 * - 1.800 |
R-factor | 0.183 * |
Rwork | 0.165 |
R-free | 0.22600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zap |
RMSD bond length | 0.011 * |
RMSD bond angle | 0.764 * |
Data reduction software | SAINT |
Data scaling software | SAINT |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 1.800 |
Rmerge | 0.068 * |
Total number of observations | 215435 * |
Number of reflections | 32636 * |
<I/σ(I)> | 19 |
Completeness [%] | 93.0 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 20 * | VAPOR DIFFUSION BY HANGING DROPS. 0.1 M SODIUM ACETATE, 20% ETHANOL, 1:1 WITH WATER SOLUTION OF THE PROTEIN (30 MG/ML)., pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 0.1 (M) | |
3 | 1 | reservoir | ethanol | 20 (%) |