5E1L
Structural and functional analysis of the E. coli FtsZ interacting protein, ZapC, reveals insight into molecular properties of a novel Z ring stabilizing protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-12-21 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 65.976, 46.741, 62.910 |
Unit cell angles | 90.00, 105.74, 90.00 |
Refinement procedure
Resolution | 37.643 - 2.150 |
R-factor | 0.2003 |
Rwork | 0.197 |
R-free | 0.23120 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.468 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.500 | |
High resolution limit [Å] | 2.150 | |
Rmerge | 0.234 | |
Number of reflections | 9961 | |
<I/σ(I)> | 11.5 | 4.6 |
Completeness [%] | 98.0 | |
Redundancy | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 1.5 M sodium citrate, 0.1 M cacodylate pH 6.5 |