1BXO
ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20) COMPLEX WITH PHOSPHONATE INHIBITOR: METHYL CYCLO[(2S)-2-[[(1R)-1-(N-(L-N-(3-METHYLBUTANOYL)VALYL-L-ASPARTYL)AMINO)-3-METHYLBUT YL] HYDROXYPHOSPHINYLOXY]-3-(3-AMINOMETHYL) PHENYLPROPANOATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1997-11-15 |
Detector | ADSC |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 96.980, 46.650, 65.710 |
Unit cell angles | 90.00, 115.57, 90.00 |
Refinement procedure
Resolution | 10.000 - 0.950 |
R-factor | 0.0991 |
R-free | 0.12470 |
Structure solution method | OTHER |
Starting model (for MR) | 1ppl |
RMSD bond length | 0.017 |
RMSD bond angle | 0.034 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 0.980 |
High resolution limit [Å] | 0.950 | 0.950 |
Rmerge | 0.053 | 0.160 |
Total number of observations | 430728 * | |
Number of reflections | 156181 * | |
<I/σ(I)> | 3.9 | 0.036 |
Completeness [%] | 98.0 | 53.8 |
Redundancy | 2.76 | 1.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 | 0.1 M CH3COONA 35% AMMONIUM SULFATE PH 4.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 35 (%) | |
3 | 1 | reservoir | sodium acetate | 100 (mM) |