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2NR9

Crystal structure of GlpG, Rhomboid Peptidase from Haemophilus influenzae

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.3.1
Synchrotron siteALS
Beamline8.3.1
Temperature [K]100
Detector technologyCCD
Collection date2005-07-14
DetectorADSC QUANTUM 210
Wavelength(s)1.11587
Spacegroup nameC 1 2 1
Unit cell lengths121.288, 35.047, 52.931
Unit cell angles90.00, 104.02, 90.00
Refinement procedure
Resolution25.000 - 2.200
R-factor0.23591
Rwork0.233
R-free0.29535
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2ic8
RMSD bond length0.005
RMSD bond angle0.992
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000
High resolution limit [Å]2.1002.100
Rmerge0.0480.590
Number of reflections12248
<I/σ(I)>13.51.85
Completeness [%]94.993.7
Redundancy1.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP629825% PEG4000, 0.1M Citrate, pH 6.0, 0.8M Ammonium Acetate, 15% Glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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