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1LC3

Crystal Structure of a Biliverdin Reductase Enzyme-Cofactor Complex

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 5.0.2
Synchrotron siteALS
Beamline5.0.2
Temperature [K]100
Detector technologyCCD
Collection date2001-12-13
DetectorADSC QUANTUM 4
Wavelength(s)1.0
Spacegroup nameP 21 21 21
Unit cell lengths51.780, 76.140, 75.010
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution30.000

*

- 1.500
Rwork0.214
R-free0.23800

*

Structure solution methodMIR
RMSD bond length0.006
RMSD bond angle22.200

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSOLVE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000

*

1.550
High resolution limit [Å]1.5001.500
Rmerge0.072

*

0.389

*

Total number of observations131242

*

Number of reflections47157
Completeness [%]97.296.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP10.54

*

2.0 M Na+/K+ phosphate, 100 mM CAPS, 200 mM lithium sulfate (Emerald Screen Wizard-I condition 27), pH 10.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6.5 (mg/ml)
21reservoirsodium potassium phosphate2.0 (M)
31reservoirCAPS100 (mM)pH10.5
41reservoirlithium sulfate200 (mM)

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PDB entries from 2024-05-15

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