7C1B
Crystal structure of a dinucleotide-binding protein (F79A/Y224A/Y246A and deletion of residues 50-75) of ABC transporter (unbound form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2019-12-08 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.930, 55.470, 124.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 62.200 - 2.300 |
R-factor | 0.1986 |
Rwork | 0.195 |
R-free | 0.26950 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7c0f |
RMSD bond length | 0.013 |
RMSD bond angle | 1.821 |
Data reduction software | MOSFLM (7.2.2) |
Data scaling software | Aimless (0.7.4) |
Phasing software | PHASER (2.8.3) |
Refinement software | REFMAC (5.8.0266) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 62.200 | 62.200 | 2.380 |
High resolution limit [Å] | 2.300 | 8.910 | 2.300 |
Rmerge | 0.150 | 0.054 | 0.559 |
Rmeas | 0.157 | 0.058 | 0.586 |
Rpim | 0.048 | 0.018 | 0.177 |
Total number of observations | 181309 | 3199 | 17280 |
Number of reflections | 16950 | 358 | 1607 |
<I/σ(I)> | 11.5 | 23.2 | 4.1 |
Completeness [%] | 100.0 | 99.9 | 100 |
Redundancy | 10.7 | 8.9 | 10.8 |
CC(1/2) | 0.997 | 0.999 | 0.928 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 277 | 0.2M ammonium sulphate, 0.1M sodium cacodylate pH 6.5, 30% PEG 8000 |