4V81

The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	PIXEL
Collection date	2008-09-12
Detector	PSI PILATUS 6M
Wavelength(s)	1.0001
Spacegroup name	P 1
Unit cell lengths	159.100, 162.540, 268.100
Unit cell angles	85.23, 81.15, 61.17

Refinement procedure

Resolution	89.946 - 3.800
R-factor	0.3089
Rwork	0.307
R-free	0.34430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1q3q
RMSD bond length	0.003
RMSD bond angle	0.678
Data reduction software	XDS
Data scaling software	XDS
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	90.000	4.000
High resolution limit [Å]	3.800	3.800
Number of reflections	209755
<I/σ(I)>	8.4	1.92
Completeness [%]	91.6	93.2
Redundancy	1.86

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	Prior to crystallisation CCT was complexed to alpha-Actin and Plp2 and purified as described (Altschuler et al., 2009, Febs Letters, 583, 782-786) and crystallised in hanging drops in the presence of ATP and Beryllium Fluoride, which was added as BeSO4 and KF. Equilibration buffer contained 100 mM Hepes pH 7.6, 50 mM MgCl2, 300 mM Na2SeO4, 6% PEG8k,1.0 mM TCEP, and 20% glycerol. Note that in the drop, protein at 4.3 mg/ml was mixed with equal amounts of equilibration buffer lacking glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 277K