1FY2
Aspartyl Dipeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-06-06 |
Detector | BRANDEIS |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 91.986, 42.690, 62.496 |
Unit cell angles | 90.00, 106.06, 90.00 |
Refinement procedure
Resolution | 20.000 * - 1.200 |
R-factor | 0.218 * |
Rwork | 0.218 |
R-free | 0.23000 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.620 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.047 | 0.274 |
Total number of observations | 137483 * | |
Number of reflections | 68270 | |
<I/σ(I)> | 14 | |
Completeness [%] | 93.6 | 76.1 |
Redundancy | 2 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 9.5 * | 293 | Conlin, C.A., (1994) J.Bacteriol., 176, 166. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6-12 (mg/ml) | |
2 | 1 | drop | CHES | 50 (mM) | |
3 | 1 | drop | cacodylate-NaOH | 50 (mM) | |
4 | 1 | drop | 1 (mM) | ||
5 | 1 | drop | PEG35000 | 2.5 (%) | |
6 | 1 | reservoir | CHES | 50 (mM) | |
7 | 1 | reservoir | 0.25 (M) |