3VKE
Contribution of the first K-homology domain of poly(C)-binding protein 1 to its affinity and specificity for C-rich oligonucleotides
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-03-05 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9801 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.597, 114.887, 43.429 |
Unit cell angles | 90.00, 93.73, 90.00 |
Refinement procedure
Resolution | 27.160 - 1.770 |
R-factor | 0.1636 |
Rwork | 0.161 |
R-free | 0.21340 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ztg |
RMSD bond length | 0.027 |
RMSD bond angle | 2.243 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 38.510 |
High resolution limit [Å] | 1.770 |
Rmerge | 0.090 |
Number of reflections | 36143 |
<I/σ(I)> | 7.9 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.2 | 293 | 0.1M phosphate-citrate, 40%(v/v) PEG 300, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |