5N29

An improved model of the Trypanosoma brucei CTP synthase glutaminase domain:acivicin complex.


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, SITTING DROP293CRYSTALLIZATION CONDITIONS: 0.15 M POTASSIUM BROMIDE, 30 % PEG MONOMETHYL ETHER 2000
Crystal Properties
Matthews coefficientSolvent content
2.738.4

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 50.48α = 90
b = 63.68β = 90
c = 76.58γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC QUANTUM 315Mirrors2008-12-11MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONDIAMOND BEAMLINE I030.98004DiamondI03

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
12.1201000.0813.97.8414866

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 REPLACEMENTTHROUGHOUT2.1201408774099.10.193460.191210.23528RANDOM18.877
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]
-0.351.02-0.67
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg33.742
r_dihedral_angle_4_deg15.604
r_dihedral_angle_3_deg12.965
r_dihedral_angle_1_deg5.52
r_long_range_B_refined3.876
r_long_range_B_other3.792
r_scangle_other2.079
r_mcangle_it1.976
r_mcangle_other1.975
r_angle_refined_deg1.232
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg33.742
r_dihedral_angle_4_deg15.604
r_dihedral_angle_3_deg12.965
r_dihedral_angle_1_deg5.52
r_long_range_B_refined3.876
r_long_range_B_other3.792
r_scangle_other2.079
r_mcangle_it1.976
r_mcangle_other1.975
r_angle_refined_deg1.232
r_scbond_it1.225
r_scbond_other1.224
r_mcbond_it1.147
r_mcbond_other1.146
r_angle_other_deg0.912
r_chiral_restr0.066
r_bond_refined_d0.008
r_gen_planes_refined0.004
r_bond_other_d0.002
r_gen_planes_other0.001
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_scangle_it
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms2091
Nucleic Acid Atoms
Solvent Atoms126
Heterogen Atoms3

Software

Software
Software NamePurpose
REFMACrefinement