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1O0Q

Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM30A
Synchrotron siteESRF
BeamlineBM30A
Temperature [K]100
Detector technologyCCD
Collection date2002-04-04
DetectorMARRESEARCH
Wavelength(s)0.98
Spacegroup nameH 3
Unit cell lengths179.900, 179.900, 37.300
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution50.000 - 2.200
R-factor0.191
Rwork0.189
R-free0.23700
Structure solution methodFOURIER SYNTHESIS
RMSD bond length0.009
RMSD bond angle1.560
Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.9002.320
High resolution limit [Å]2.2002.200
Rmerge0.099

*

0.241

*

Total number of observations81355

*

Number of reflections22772
Completeness [%]99.799.9
Redundancy3.63.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP74

*

Villeret, V., (1997) Protein Sci., 6, 2462.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirammonium sulfate1.6 (M)
21reservoirHEPES0.1 (M)pH7.0
31dropprotein15 (mg/ml)

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