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1GN1

crystal structure of the mouse CCT gamma apical domain (monoclinic)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
Collection date2000-11-15
DetectorADSC CCD
Spacegroup nameP 1 21 1
Unit cell lengths60.244, 234.229, 62.703
Unit cell angles90.00, 114.70, 90.00
Refinement procedure
Resolution29.110 - 2.800
R-factor0.238
Rwork0.238
R-free0.28700

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gml
RMSD bond length0.010
RMSD bond angle1.340

*

Data reduction softwareMOSFLM
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]29.000

*

2.940
High resolution limit [Å]2.8002.800
Rmerge0.0510.147
Number of reflections33738

*

<I/σ(I)>6.34.7
Completeness [%]85.274.1
Redundancy2.12
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Batch method

*

6.514

*

CRYSTALS GROWN BY MICROBATCH METHOD (UNDER OIL) USING A 1:1 MIXTURE OF 30MG/ML PROTEIN, 400MM NACL, 20% GLYCEROL, 8MM TRIS PH8.0, 0.4MM EDTA AND 14% PEG 8K, 100MM NA-CACODYLATE PH6.5, 40MM CA(OAC)2, 40% GLYCEROL, pH 6.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein30 (mg/ml)
211Tris8 (mM)pH8.0
311400 (mM)
411EDTA0.4 (mM)
511glycerol20 (%)
611sodium cacodylate100 (mM)pH6.5
711PEG800014 (%(w/v))
81140 (mM)
911glycerol40 (%)

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PDB entries from 2024-09-18

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