4UYS

X-ray structure of the N-terminal domain of the flocculin Flo11 from Saccharomyces cerevisiae


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.5PROTEIN WAS CRYSTALLIZED FROM 100 MM NAHEPES, PH 7.5, 100 MM MGCL2, 30% PEG 400, THEN SOAKED IN THIS CONDITION CONTAINING 50 MM CACL2 ADDITIONALLY FOR 5 MIN; FOR CRYOPROTECTION THE PROTEIN WAS SOAKED IN THE LATTER CONDITION CONTAINING 35% PEG 400 INSTEAD OF 30%.
Crystal Properties
Matthews coefficientSolvent content
2.2545.45

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 52.72α = 90
b = 101.55β = 90
c = 33.87γ = 90
Symmetry
Space GroupP 21 21 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100PIXELDECTRIS PILATUS 6MMIRRORS2013-08-03MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONBESSY BEAMLINE 14.1BESSY14.1

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
11.0528.51000.0611.45.885769-3
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)
11.051.1199.90.622.55.3

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 REPLACEMENTTHROUGHOUT1.0528.5184603108199.910.14710.146830.16968RANDOM12.7
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]
1.68-1.45-0.23
RMS Deviations
KeyRefinement Restraint Deviation
r_sphericity_free84.443
r_dihedral_angle_2_deg36.38
r_sphericity_bonded12.101
r_dihedral_angle_3_deg10.555
r_dihedral_angle_1_deg6.8
r_rigid_bond_restr2.5
r_scbond_it1.6
r_angle_refined_deg1.593
r_mcangle_it1.232
r_mcbond_it0.956
RMS Deviations
KeyRefinement Restraint Deviation
r_sphericity_free84.443
r_dihedral_angle_2_deg36.38
r_sphericity_bonded12.101
r_dihedral_angle_3_deg10.555
r_dihedral_angle_1_deg6.8
r_rigid_bond_restr2.5
r_scbond_it1.6
r_angle_refined_deg1.593
r_mcangle_it1.232
r_mcbond_it0.956
r_mcbond_other0.954
r_angle_other_deg0.925
r_chiral_restr0.109
r_bond_refined_d0.011
r_gen_planes_refined0.008
r_gen_planes_other0.002
r_bond_other_d0.001
r_dihedral_angle_4_deg
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_mcangle_other
r_scbond_other
r_scangle_it
r_scangle_other
r_long_range_B_refined
r_long_range_B_other
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms1416
Nucleic Acid Atoms
Solvent Atoms280
Heterogen Atoms8

Software

Software
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
PHENIXphasing