1VE6

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.1 Å)

Cell axes64.730104.739170.944
Cell angles90.0090.0090.00
SpacegroupP 21 21 21
Resolution limits29.77 - 2.10
the highest resolution shell value2.230 - 2.100
R-factor0.207
R-work0.19300
the highest resolution shell value0.192
R-free0.22900
the highest resolution shell value0.255
RMSD bond length0.010
RMSD bond angle1.600

Data Collection Statistics

Resolution limits50.00 - 2.10
the highest resolution shell value -
Number of reflections118700
Rmerge_l_obs0.079
the highest resolution shell value0.212
Completeness99.2
Redundancy7.4
the highest resolution shell value7.2
I/sigma(I)-3

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP4.6291

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*