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Crystal structure of truncated bacteriophage hyaluronan lyase HylP in complex with unsaturated hyaluronan tetra-saccharides

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 24-ID-E
Synchrotron siteAPS
Beamline24-ID-E
Temperature [K]100
Detector technologyCCD
Collection date2012-05-29
DetectorADSC QUANTUM 315r
Wavelength(s)0.97949
Spacegroup nameP 21 21 21
Unit cell lengths67.535, 86.819, 168.646
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution38.680 - 2.200
R-factor0.1839
Rwork0.182
R-free0.21040
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)6wv2
RMSD bond length0.009
RMSD bond angle1.307
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareREFMAC (5.8.0189)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0002.280
High resolution limit [Å]2.2002.200
Rmerge0.0810.559
Number of reflections511695022
<I/σ(I)>11.24.6
Completeness [%]99.8100
Redundancy8.18.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.529310% (v/v) 2-Propanol, 20% (w/v) PEG 4000, 0.1 M Hepes, pH 7.5; incubation of protein HylP with unsaturated Hyaluronan tetra-saccharides at 1:20 molar ratio prior to crystallization

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