2MEG

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (1.8 Å)

Cell axes57.10061.06033.760
Cell angles90.0090.0090.00
SpacegroupP 21 21 21
Resolution limits8.00 - 1.80
the highest resolution shell value1.880 - 1.800
R-factor0.151
R-work0.15100
the highest resolution shell value0.212
RMSD bond length0.008
RMSD bond angle1.520 (23.900*)

Data Collection Statistics

Resolution limits - 1.80
the highest resolution shell value1.90* -
Number of reflections42094 (10582*)
Number of measurements42094*
Rmerge_l_obs0.052
the highest resolution shell value0.180
Completeness92.2
Redundancy2.5
I/sigma(I)1

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1Vapor diffusion, hanging drop*4.510**

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.