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1LOK

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 14-BM-C
Synchrotron siteAPS
Beamline14-BM-C
Temperature [K]100
Detector technologyCCD
Collection date2000-02-11
DetectorADSC QUANTUM 4
Wavelength(s)1.0000
Spacegroup nameP 61 2 2
Unit cell lengths108.338, 108.338, 93.519
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000

*

- 1.200
R-factor0.145
Rwork0.158
R-free0.17600

*

Structure solution methodFOURIER SYNTHESIS
Starting model (for MR)1amp
RMSD bond length0.018
RMSD bond angle0.032
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareSHELXL-97
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000

*

1.250
High resolution limit [Å]1.200

*

1.200

*

Rmerge0.057

*

0.290

*

Total number of observations1348266

*

Number of reflections117248

*

Completeness [%]99.0

*

98
Redundancy15
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

8295Tris, potassium thiocyanate, sodium chloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein16 (mg/ml)
21dropTris10 (mM)pH8.0
31dropKSCN10 (mM)
41drop0.4 (M)
51reservoirTris100 (mM)pH8.0
61reservoirKSCN100 (mM)
71reservoir4.5 (M)

218853

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