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1H2X

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y473F MUTANT

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2000-06-15
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths71.200, 99.800, 111.100
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution26.000 - 1.490
R-factor0.175
Rwork0.175
R-free0.19600
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qfm
RMSD bond length0.007
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]26.0001.540
High resolution limit [Å]1.4901.490
Rmerge0.0360.097
Total number of observations545342

*

Number of reflections128812
<I/σ(I)>37.29.6
Completeness [%]99.497.3
Redundancy4.23.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.54

*

Fulop, V., (1998) Cell, 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)

223790

PDB entries from 2024-08-14

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