4QBU

Structure of the Acyl Transferase domain of ZmaA


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, HANGING DROP5.5298mother liquor 200 mM MgCl2, 20% PEG 4000, 800 mM sodium formate, 100 mM BisTris; drops equal volume 7 mg/ml protein and mother liquor, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystal Properties
Matthews coefficientSolvent content
2.1442.41

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 46.915α = 90
b = 74.25β = 90
c = 124.728γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATEMAR scanner 300 mm plate2009-05-06MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONAPS BEAMLINE 21-ID-D0.97872APS21-ID-D

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Sym 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
11.652599.90.04927.76.9544475438220.8
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R-Sym I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
11.651.681000.3634.162669

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (High)Resolution (Low)Number Reflections (All)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (All)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONSAD + molecular replacementTHROUGHOUT2QO31.724.514636446276247899.810.172570.172570.171080.20046RANDOM22.131
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]
-0.10.060.04
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg31.693
r_dihedral_angle_4_deg16.743
r_dihedral_angle_3_deg12.954
r_long_range_B_refined5.561
r_dihedral_angle_1_deg5.382
r_scbond_it2.674
r_angle_refined_deg1.706
r_mcangle_it1.581
r_mcbond_it1.049
r_chiral_restr0.122
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg31.693
r_dihedral_angle_4_deg16.743
r_dihedral_angle_3_deg12.954
r_long_range_B_refined5.561
r_dihedral_angle_1_deg5.382
r_scbond_it2.674
r_angle_refined_deg1.706
r_mcangle_it1.581
r_mcbond_it1.049
r_chiral_restr0.122
r_bond_refined_d0.019
r_gen_planes_refined0.01
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_refined
r_nbd_other
r_nbtor_refined
r_nbtor_other
r_xyhbond_nbd_refined
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_refined
r_symmetry_vdw_other
r_symmetry_hbond_refined
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_it
r_scangle_other
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 Atoms3515
Nucleic Acid Atoms
Solvent Atoms276
Heterogen Atoms3

Software

Software
Software NamePurpose
Auto-Rickshawphasing
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling