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5OF1

The structural versatility of TasA in B. subtilis biofilm formation

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsBESSY BEAMLINE 14.1
Synchrotron siteBESSY
Beamline14.1
Temperature [K]100
Detector technologyPIXEL
Collection date2015-06-23
DetectorDECTRIS PILATUS 6M
Wavelength(s)0.9797
Spacegroup nameP 1
Unit cell lengths40.728, 43.149, 51.744
Unit cell angles89.92, 91.86, 90.01
Refinement procedure
Resolution40.710 - 1.560
R-factor0.15273
Rwork0.152
R-free0.17523
Structure solution methodSAD
RMSD bond length0.016
RMSD bond angle1.842
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareAutoSol
Refinement softwareREFMAC (5.8.0151)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.7101.614
High resolution limit [Å]1.5601.560
Rmerge0.0780.416
Number of reflections473684658
<I/σ(I)>13.332.73
Completeness [%]96.393.31
Redundancy4.14.2
CC(1/2)0.9960.921
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP4.8293.1534% PEG2000 MME, 0.2M lithium salicylate, 0.1M ammonium sulfate, 0.1M sodium acetate pH 4.8

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