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1QFX

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM1A
Synchrotron siteESRF
BeamlineBM1A
Temperature [K]120
Detector technologyIMAGE PLATE
Collection date1997-01-29
DetectorMARRESEARCH
Spacegroup nameP 61 2 2
Unit cell lengths170.600, 170.600, 201.150
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution25.000 - 2.400
R-factor0.18

*

Rwork0.183
R-free0.22500
Structure solution methodSIRAS
RMSD bond length0.011
RMSD bond angle1.600
Data reduction softwareXDS
Data scaling softwareXDS
Phasing softwareSHELXS
Refinement softwareX-PLOR (3.851)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.500
High resolution limit [Å]2.4002.400
Rmerge0.055

*

0.182

*

Total number of observations173451

*

Number of reflections58656
<I/σ(I)>18.84.2
Completeness [%]86.567.3
Redundancy2.91.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

70.1M HEPES/HCL PH 7.0, 2.4M AMMONIUM SULFATE
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6 (mg/ml)
21reservoirammonium sulfate2.4 (M)
31reservoirHEPES100 (mM)

217705

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