1ARM

CARBOXYPEPTIDASE A WITH ZN REPLACED BY HG


X-RAY DIFFRACTION

Crystallization

Crystal Properties
Matthews coefficientSolvent content
2.141.47

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 51.7α = 90
b = 60.32β = 97.39
c = 47.2γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-rayIMAGE PLATEMACSCIENCE DIP1001990-04-17M
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1

Data Collection

Refinement

Statistics
Diffraction IDStructure Solution MethodResolution (High)Resolution (Low)Number Reflections (All)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-WorkR-FreeMean Isotropic B
X-RAY DIFFRACTION1.7612.1267512675191
Temperature Factor Modeling
Anisotropic B[1][1]Anisotropic B[1][2]Anisotropic B[1][3]Anisotropic B[2][2]Anisotropic B[2][3]Anisotropic B[3][3]
RMS Deviations
KeyRefinement Restraint Deviation
t_dihedral_angle_d16.1
t_it7.84
t_angle_deg2.76
t_nbd0.04
t_bond_d0.017
t_gen_planes0.017
t_trig_c_planes0.013
t_incorr_chiral_ct
t_pseud_angle
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms2436
Nucleic Acid Atoms
Solvent Atoms217
Heterogen Atoms13

Software

Software
Software NamePurpose
TNTrefinement
PROLSQrefinement
P.A.TUCKERdata collection
P.A.TUCKERdata reduction