1ZGB

Crystal Structure of Torpedo Californica Acetylcholinesterase in Complex With an (R)-Tacrine(10)-Hupyridone Inhibitor.


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1277PEG 200, pH 5.8, temperature 277K, VAPOR DIFFUSION, HANGING DROP. PROTEIN WAS CRYSTALLISED FROM 28% V/V PEG 200 0.5 M MES PH 5.8 AT 277K, SEEDING WITH TRIGONAL MICROCRYSTALS; THEN SOAKED IN MOTHER LIQUOR (40% V/V PEG 200 IN 0.1 M MES BUFFER, PH 5.8) CONTAINING 2 MM (RS)-(+/-)- TACRINE(10)-HUPYRIDONE ((5RS)-(+/-)-5-{[10-(1,2,3,4-TETRAHYDROACRIDIN-9-YLAMINO) DECYL] AMINO}-5,6,7,8-TETRAHYDRO-QUINOLIN-2(1H)-ONE) BIS-OXALATE FOR 17 HOURS.
Crystal Properties
Matthews coefficientSolvent content
4.0769.7

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 111.449α = 90
b = 111.449β = 90
c = 137.095γ = 120
Symmetry
Space GroupP 31 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray120IMAGE PLATERIGAKU RAXIS IVOSMIC BLUE CONFOCAL MIRRORS2000-09-07MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RUH3R

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Merge I (Observed)Net I Over Average Sigma (I)RedundancyNumber Reflections (All)Number Reflections (Observed)Observed Criterion Sigma (F)Observed Criterion Sigma (I)B (Isotropic) From Wilson Plot
12.33098.50.06821.91.594425028.8
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R Merge I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
12.32.3899.70.3675.1610

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT2.329.1943555219098.40.1880.1880.23RANDOM39.3
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]
7.665.567.66-15.32
RMS Deviations
KeyRefinement Restraint Deviation
c_dihedral_angle_d24.1
c_scangle_it3.028
c_scbond_it2.169
c_mcangle_it1.959
c_angle_deg1.9
c_improper_angle_d1.38
c_mcbond_it1.267
c_bond_d0.116
c_bond_d_na
c_bond_d_prot
RMS Deviations
KeyRefinement Restraint Deviation
c_dihedral_angle_d24.1
c_scangle_it3.028
c_scbond_it2.169
c_mcangle_it1.959
c_angle_deg1.9
c_improper_angle_d1.38
c_mcbond_it1.267
c_bond_d0.116
c_bond_d_na
c_bond_d_prot
c_angle_d
c_angle_d_na
c_angle_d_prot
c_angle_deg_na
c_angle_deg_prot
c_dihedral_angle_d_na
c_dihedral_angle_d_prot
c_improper_angle_d_na
c_improper_angle_d_prot
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms4175
Nucleic Acid Atoms
Solvent Atoms178
Heterogen Atoms65

Software

Software
Software NamePurpose
CNSrefinement
STRATEGYdata reduction
CCP4data scaling
XTALVIEWrefinement