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2GNX

X-ray structure of a hypothetical protein from Mouse Mm.209172

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyCCD
Collection date2005-07-10
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.97182
Spacegroup nameC 2 2 21
Unit cell lengths82.687, 198.962, 67.076
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution40.970 - 2.450
Rwork0.281
R-free0.32200
Structure solution methodSAD
RMSD bond length0.008
RMSD bond angle1.200
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]40.9662.540
High resolution limit [Å]2.4502.450
Rmerge0.0700.682
Number of reflections35469
<I/σ(I)>12.8961.697
Completeness [%]91.871.4
Redundancy9.45.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP293PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 MES PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (0.003 SODIUM CHLORIDE, 0.10 M HEPES PH 7.5) Crystals cryo-protected with Fomblin followed by Paratone N, vapor diffusion, hanging drop, temperature 293K
1VAPOR DIFFUSION, HANGING DROP293PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 MES PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (0.003 SODIUM CHLORIDE, 0.10 M HEPES PH 7.5) Crystals cryo-protected with Fomblin followed by Paratone N, vapor diffusion, hanging drop, temperature 293K

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