2CNM

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
15.515% PEG400 (W/V), 100 MM NACITRATE PH 5.5, 100 MM (NH4)2SO4
Crystal Properties
Matthews coefficientSolvent content
3.160.3

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 133.127α = 90
b = 133.127β = 90
c = 190.986γ = 120
Symmetry
Space GroupH 3 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray93IMAGE PLATEMARRESEARCH RAXIS IVOSMIC CONFOCAL MAXFLUX OPTICSMSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RU200B

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
12.6401000.0719.44.419233
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)
12.62.671000.324.54.4

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 DIFFRACTIONSIRASTHROUGHOUT2.698.531923310371000.1960.1930.257RANDOM28.56
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]
0.550.270.55-0.82
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg40.073
r_dihedral_angle_3_deg16.091
r_dihedral_angle_4_deg15.605
r_dihedral_angle_1_deg6.192
r_scangle_it2.899
r_scbond_it1.761
r_angle_refined_deg1.602
r_mcangle_it1.02
r_mcbond_it0.584
r_symmetry_vdw_refined0.326
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg40.073
r_dihedral_angle_3_deg16.091
r_dihedral_angle_4_deg15.605
r_dihedral_angle_1_deg6.192
r_scangle_it2.899
r_scbond_it1.761
r_angle_refined_deg1.602
r_mcangle_it1.02
r_mcbond_it0.584
r_symmetry_vdw_refined0.326
r_nbtor_refined0.314
r_nbd_refined0.211
r_symmetry_hbond_refined0.151
r_xyhbond_nbd_refined0.145
r_chiral_restr0.103
r_bond_refined_d0.014
r_gen_planes_refined0.005
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 Atoms3801
Nucleic Acid Atoms
Solvent Atoms60
Heterogen Atoms144

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
SOLVEphasing