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1O6G

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641N MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]100
Detector technologyCCD
Collection date2001-05-15
DetectorADSC CCD
Spacegroup nameP 21 21 21
Unit cell lengths71.600, 100.600, 111.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000 - 1.400
R-factor0.2
Rwork0.200
R-free0.21600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qfm
RMSD bond length0.008
RMSD bond angle1.400
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCCP4
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.450
High resolution limit [Å]1.4001.400
Rmerge0.0530.209
Total number of observations686744

*

Number of reflections156733
<I/σ(I)>25.84.7
Completeness [%]99.197.5
Redundancy4.43.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.54

*

Fulop, V., (1998) Cell(Cambridge,Mass.), 94, 161.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirmPEG500017 (%(w/v))
21reservoirglycerol15 (%(v/v))
31reservoirmonothioglycerol1 (%(v/v))
41reservoir20 (mM)
51reservoirTris100 (mM)
61dropprotein10 (mg/ml)

219869

PDB entries from 2024-05-15

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