216L

STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Replaces:  116L

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.1 Å)

Cell axes116.50054.40059.500
Cell angles90.00102.3090.00
SpacegroupC 1 2 1
Resolution limits - 2.10
the highest resolution shell value -
R-factor0.194
RMSD bond length0.017
RMSD bond angle2.500

Data Collection Statistics

Resolution limits -
the highest resolution shell value -

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
1111.05 (M)
2111.26 (M)
3110.23 (M)
411beta-mercaptoethanol1.4 (mM)
Annotated Information is extracted from Literature Info*
S. Dao-pin, (1990) Proteins Struct. Funct. Gen., 7, 198.