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2VO9

CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500

Replaces:  1XP2
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2004-09-24
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths59.787, 95.180, 182.578
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 1.800
R-factor0.198
Rwork0.196
R-free0.24400
Structure solution methodSAD
Starting model (for MR)NONE
RMSD bond length0.018
RMSD bond angle1.628
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareHKL2Map
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.900
High resolution limit [Å]1.8001.800
Rmerge0.0600.240
Number of reflections46838
<I/σ(I)>9.583.66
Completeness [%]96.796.7
Redundancy3.33.66
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.52980.1M HEPES, 2.4% PEG 400, 1.7M (NH4)2SO4, PH 7.5, VAPOR DIFFUSION, HANGING DROP, 298K

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