1AGY
The 1.15 angstrom refined structure of fusarium solani pisi cutinase
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 288 |
Detector technology | AREA DETECTOR |
Collection date | 1993-01 |
Detector | NICOLET |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 35.120, 67.360, 37.050 |
Unit cell angles | 90.00, 93.90, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.150 |
R-factor | 0.175 |
Rwork | 0.175 |
R-free | 0.19700 |
Structure solution method | RESOLUTION EXTENSION |
Starting model (for MR) | CUTINASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION |
RMSD bond length | 0.019 |
RMSD bond angle | 59.960 * |
Data reduction software | MARSCALE |
Data scaling software | XDS |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.200 |
High resolution limit [Å] | 1.150 | 1.150 |
Rmerge | 0.010 | 0.030 |
Number of reflections | 60972 | |
<I/σ(I)> | 27.46 | 3.21 |
Completeness [%] | 95.2 | 84.2 |
Redundancy | 4.09 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 20 * | Abergel, C., (1990) J. Mol. Biol., 215, 215. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | HEPES | 0.1 (M) | |
3 | 1 | reservoir | PEG1000 | 15-20 (%(w/v)) |