2CE8

An EH1 peptide bound to the Groucho-TLE WD40 domain.


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1MICROBATCH6.52876MG/ML PROTEIN WAS MIXED 1:1 WITH 12% PEG8000 100MM NACACODYLATE, 100MM CAACETATE AT 14C IN MICROBATCH. PEPTIDES WERE ADDED TO THE PROTEIN CRYSTALS IN 125 MM NACL, 25 MM TRIS PH8.0, 0.5 MM EDTA TO A FINAL CONCENTRATION OF 0.76 MM, AND INCUBATED FOR 16 H BEFORE HARVESTING AND WASHING IN 50MM NA CACODYLATE PH6.5, 12 % PEG 8K, AND CRYO-PROTECTED IN 30% ETHYLENE GLYCOL 50MM NA CACODYLATE PH6.5, 12 % PEG 8K, pH 6.50
Crystal Properties
Matthews coefficientSolvent content
2.550

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 107.585α = 90
b = 56.352β = 112.32
c = 125.245γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATEMARRESEARCHOSMIC MIRRORS2005-09-02MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RU300

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
12.0230950.0613.52.987651
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)
12.022.1274.50.195.22.5

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (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 REPLACEMENTTHROUGHOUTPDB ENTRY 1GXR2.03116.2583258438096.40.1820.1790.238RANDOM20.22
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]
-0.84-0.29-0.140.75
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.469
r_dihedral_angle_4_deg20.331
r_dihedral_angle_3_deg15.59
r_dihedral_angle_1_deg8.24
r_scangle_it3.908
r_scbond_it2.627
r_mcangle_it1.872
r_angle_refined_deg1.804
r_mcbond_it1.126
r_nbtor_refined0.304
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.469
r_dihedral_angle_4_deg20.331
r_dihedral_angle_3_deg15.59
r_dihedral_angle_1_deg8.24
r_scangle_it3.908
r_scbond_it2.627
r_mcangle_it1.872
r_angle_refined_deg1.804
r_mcbond_it1.126
r_nbtor_refined0.304
r_symmetry_hbond_refined0.233
r_nbd_refined0.225
r_symmetry_vdw_refined0.206
r_xyhbond_nbd_refined0.182
r_chiral_restr0.13
r_bond_refined_d0.018
r_gen_planes_refined0.007
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_other
r_nbtor_other
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_other
r_mcangle_other
r_scbond_other
r_scangle_other
r_long_range_B_refined
r_long_range_B_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms10488
Nucleic Acid Atoms
Solvent Atoms1077
Heterogen Atoms

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing