2PZG
Minimal human CFTR first nucleotide binding domain as a monomer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-17 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.9796 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.417, 81.498, 99.304 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.907 - 1.800 |
R-factor | 0.204 |
Rwork | 0.203 |
R-free | 0.23370 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pze |
RMSD bond length | 0.011 |
RMSD bond angle | 1.305 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 24.909 | 24.910 | 1.900 |
High resolution limit [Å] | 1.800 | 5.690 | 1.800 |
Rmerge | 0.077 | 0.036 | 0.781 |
Total number of observations | 10461 | 43338 | |
Number of reflections | 47606 | ||
<I/σ(I)> | 6.5 | 15.1 | 1 |
Completeness [%] | 99.8 | 97.4 | 99.8 |
Redundancy | 6.8 | 6.5 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 281 | Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 6.5, 25% PEG 10K ; Cryo: 25% glycerol, vapor diffusion, temperature 281K |