3BZD
Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-03-15 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 65 |
Unit cell lengths | 96.970, 96.970, 92.510 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 27.990 - 2.300 |
R-factor | 0.213 |
Rwork | 0.210 |
R-free | 0.25800 |
RMSD bond length | 0.031 |
RMSD bond angle | 2.359 |
Data reduction software | CrystalClear |
Data scaling software | CrystalClear |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.360 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.058 | 0.356 |
Number of reflections | 21938 | |
Completeness [%] | 99.7 | 93.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 2.0 M ammonium sulfate, 0.1 M Tris-Cl pH 7.0, 0.3 % 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K |