2HEB

CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.2 Å)

Cell axes56.80061.22033.760
Cell angles90.0090.0090.00
SpacegroupP 21 21 21
Resolution limits8.00 - 2.20
the highest resolution shell value -
R-factor0.124
R-work0.12400
RMSD bond length0.008
RMSD bond angle1.520

Data Collection Statistics

Resolution limits - 2.00*
the highest resolution shell value -
Number of reflections5702
Number of measurements21591*
Rmerge_l_obs0.071
the highest resolution shell value0.185*
Completeness67.7
the highest resolution shell value56.2*
Redundancy3.87
I/sigma(I)1

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1Vapor diffusion, hanging drop*4.5*10**

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10 (mg/ml)
21reservoir2.5 (M)
31reservoiracetate20 (mM)
Annotated Information is extracted from Literature Info*
Takano, K., (1995) J.Mol.Biol., 254, 62.