2BM6 | pdb_00002bm6

The Structure of MfpA (Rv3361c, C2221 Crystal form). The Pentapeptide Repeat Protein from Mycobacterium tuberculosis Folds as A Right- handed Quadrilateral Beta-helix.


X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
TypeSourceAccession CodeDetails
experimental modelOtherPREVIOUS STRUCTURE DETERMINED BY SE-MET MAD

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
15.5PROTEIN (10 MG/ML, 10 MM AMMONIUM CITRATE PH 7.5, 30 MM BETA-MERCAPTOETHANOL) CRYSTALLIZED IN 35% 2-ETHOXYETHANOL, 100 MM CITRATE PH 5.5. CRYSTAL WAS SOAKED IN 100 MM MES PH 5.2, 30 % PEG400, 1 M CESIUM CHLORIDE PRIOR TO VITRIFICATION AND DATA COLLECTION.
Crystal Properties
Matthews coefficientSolvent content
1.8834.02

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 33.393α = 90
b = 48.573β = 90
c = 188.367γ = 90
Symmetry
Space GroupC 2 2 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray93IMAGE PLATEMSC RAXIS IVMSINGLE 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
12.23097.10.0627.76.4800424.7
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)
12.22.2892.30.1484

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-Work (Depositor)R-Work (DCC)R-Free (Depositor)R-Free (DCC)R-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUTPREVIOUS STRUCTURE DETERMINED BY SE-MET MAD2.230757542497.10.1970.1970.190.2560.25RANDOM20.5
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]
3.052-4.0340.982
RMS Deviations
KeyRefinement Restraint Deviation
c_angle_deg1.92
c_bond_d0.02
c_bond_d_na
c_bond_d_prot
c_angle_d
c_angle_d_na
c_angle_d_prot
c_angle_deg_na
c_angle_deg_prot
c_dihedral_angle_d
RMS Deviations
KeyRefinement Restraint Deviation
c_angle_deg1.92
c_bond_d0.02
c_bond_d_na
c_bond_d_prot
c_angle_d
c_angle_d_na
c_angle_d_prot
c_angle_deg_na
c_angle_deg_prot
c_dihedral_angle_d
c_dihedral_angle_d_na
c_dihedral_angle_d_prot
c_improper_angle_d
c_improper_angle_d_na
c_improper_angle_d_prot
c_mcbond_it
c_mcangle_it
c_scbond_it
c_scangle_it
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms1371
Nucleic Acid Atoms
Solvent Atoms75
Heterogen Atoms6

Software

Software
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing