4P49
The structure of a chicken anti-prostate specific antigen scFv
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-16 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.953697 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 52.459, 52.459, 302.375 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.396 - 1.400 |
R-factor | 0.1845 |
Rwork | 0.183 |
R-free | 0.21380 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.021 |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.396 | 151.188 | 1.480 |
High resolution limit [Å] | 1.400 | 4.430 | 1.400 |
Rmerge | 0.126 | 0.079 | 0.910 |
Rmeas | 0.129 | ||
Rpim | 0.029 | 0.019 | 0.313 |
Total number of observations | 887042 | 33636 | 62140 |
Number of reflections | 50126 | ||
<I/σ(I)> | 12.9 | 24.7 | 2.3 |
Completeness [%] | 99.5 | 100 | 96.3 |
Redundancy | 17.7 | 17.4 | 9.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 0.1M NaOAc pH 4.6, 0.2M NH4-sulfate |