4YBF
Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-01-06 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.915 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.138, 57.147, 54.553 |
Unit cell angles | 90.00, 90.61, 90.00 |
Refinement procedure
Resolution | 39.460 - 1.240 |
R-factor | 0.1482 |
Rwork | 0.147 |
R-free | 0.17450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3fv3 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.615 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.310 | |
High resolution limit [Å] | 1.240 | 3.700 | 1.240 |
Rmerge | 0.062 | 0.050 | 0.521 |
Rmeas | 0.068 | 0.054 | 0.569 |
Total number of observations | 554808 | ||
Number of reflections | 84475 | 3300 | 13193 |
<I/σ(I)> | 14.85 | 33.88 | 3.4 |
Completeness [%] | 98.3 | 99.1 | 95.5 |
Redundancy | 6.5 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | PEG 400 |