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5DN5

Structure of a C-terminally truncated glycoside hydrolase domain from Salmonella typhimurium FlgJ

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU MICROMAX-007 HF
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2014-06-16
DetectorRIGAKU RAXIS IV++
Wavelength(s)1.54
Spacegroup nameC 1 2 1
Unit cell lengths105.700, 61.120, 65.220
Unit cell angles90.00, 106.70, 90.00
Refinement procedure
Resolution29.756 - 2.150
R-factor0.1789
Rwork0.175
R-free0.25170
Structure solution methodSAD
RMSD bond length0.014
RMSD bond angle1.409
Data reduction softwareMOSFLM
Data scaling softwareAimless
Phasing softwarePHENIX
Refinement softwarePHENIX (1.9_1692)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]37.4702.220
High resolution limit [Å]2.1502.150
Rmerge0.1500.830
Number of reflections21763
<I/σ(I)>10.32.5
Completeness [%]99.799
Redundancy7.37.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP829335 mg/ml protein in 18-22% polyethylene glycol 3350 and 0.25-0.35 M NaI

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