4BFC
Crystal structure of the C-terminal CMP-Kdo binding domain of WaaA from Acinetobacter baumannii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-3 |
Synchrotron site | MAX II |
Beamline | I911-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-02-01 |
Detector | MARRESEARCH MAR165 |
Spacegroup name | H 3 |
Unit cell lengths | 110.370, 110.370, 70.340 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.330 - 1.700 |
R-factor | 0.13518 |
Rwork | 0.134 |
R-free | 0.16093 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2xci |
RMSD bond length | 0.019 |
RMSD bond angle | 1.885 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.800 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.050 | 0.460 |
Number of reflections | 35057 | |
<I/σ(I)> | 24.9 | 3.77 |
Completeness [%] | 99.4 | 98.8 |
Redundancy | 5.7 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 0.1M NA CITRATE BUFFER PH 6.0, 0.2 MM LITHIUM SULPHATE AND 17 TO 23 % PEG 3350 |