1WAR

Recombinant Human Purple Acid Phosphatase expressed in Pichia Pastoris


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1277THE PROTEIN (10 MG/ML) IN 50 MM MES AT PH 6, WAS PASSED THROUGH AN ULTRAFREE-MC 0.22 MM SPIN FILTER UNIT (MILLIPORE) AND ALLOWED TO STAND AT 4 DEGREES C. PURPLE CRYSTALS GREW SPONTANEOUSLY OVERNIGHT AND REACHED SIZES UP TO 0.5 MM IN SEVERAL WEEKS.
Crystal Properties
Matthews coefficientSolvent content
2.9157.7

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 80.538α = 90
b = 80.538β = 90
c = 99.998γ = 90
Symmetry
Space GroupP 43 21 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray300IMAGE PLATEMAR scanner 345 mm plateOSMIC MIRRORS2003-08-20MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU RU200

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
12.2218.9894.50.0717.974.215951-336
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)
12.222.3940.45.494.2

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-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUTPDB ENTRY 1UTE2.2218.981516776794.70.1410.1380.198RANDOM32.02
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]
-0.78-0.781.55
RMS Deviations
KeyRefinement Restraint Deviation
r_scangle_it10.013
r_scbond_it6.455
r_dihedral_angle_1_deg6.366
r_mcangle_it4.614
r_mcbond_it2.645
r_angle_refined_deg1.373
r_angle_other_deg0.862
r_symmetry_vdw_other0.254
r_nbd_other0.236
r_nbd_refined0.182
RMS Deviations
KeyRefinement Restraint Deviation
r_scangle_it10.013
r_scbond_it6.455
r_dihedral_angle_1_deg6.366
r_mcangle_it4.614
r_mcbond_it2.645
r_angle_refined_deg1.373
r_angle_other_deg0.862
r_symmetry_vdw_other0.254
r_nbd_other0.236
r_nbd_refined0.182
r_symmetry_hbond_refined0.157
r_xyhbond_nbd_refined0.149
r_nbtor_other0.081
r_chiral_restr0.077
r_symmetry_vdw_refined0.059
r_bond_refined_d0.013
r_gen_planes_refined0.005
r_bond_other_d0.002
r_gen_planes_other0.001
r_dihedral_angle_2_deg
r_dihedral_angle_3_deg
r_dihedral_angle_4_deg
r_nbtor_refined
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_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 Atoms2477
Nucleic Acid Atoms
Solvent Atoms61
Heterogen Atoms21

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing