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- PDB-9gt8: DTPAA CHIP EXPERIMENT, CRISTALLINA, X,Y SPACING 100,100 -

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Basic information

Entry
Database: PDB / ID: 9gt8
TitleDTPAA CHIP EXPERIMENT, CRISTALLINA, X,Y SPACING 100,100
ComponentsDeferrochelatase
KeywordsOXIDOREDUCTASE / PEROXIDASE / RADIATION DAMAGE / SERIAL CRYSTALLOGRAPHY
Function / homology
Function and homology information


iron import into cell / cell envelope / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / peroxidase activity / lyase activity / heme binding / metal ion binding / cytosol
Similarity search - Function
Deferrochelatase / : / : / Dyp-type peroxidase, C-terminal / Dyp-type peroxidase, N-terminal / DyP-type peroxidase family. / Dyp-type peroxidase / Dimeric alpha-beta barrel / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Deferrochelatase
Similarity search - Component
Biological speciesStreptomyces lividans 1326 (bacteria)
MethodX-RAY DIFFRACTION / FREE ELECTRON LASER / MOLECULAR REPLACEMENT / Resolution: 1.54 Å
AuthorsGorel, A. / Schlichting, I.
Funding support Germany, 1items
OrganizationGrant numberCountry
Max Planck Society Germany
CitationJournal: To Be Published
Title: Radiation damage in SOS chip experiments
Authors: Gorel, A. / Schlichting, I.
History
DepositionSep 17, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Deferrochelatase
B: Deferrochelatase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,9194
Polymers78,6862
Non-polymers1,2332
Water12,538696
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)72.600, 68.200, 73.900
Angle α, β, γ (deg.)90.00, 105.50, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Deferrochelatase / Peroxidase EfeB


Mass: 39343.094 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces lividans 1326 (bacteria) / Gene: SLI_2602 / Production host: Escherichia coli (E. coli)
References: UniProt: A0A7U9DT46, Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases
#2: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 696 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.24 Å3/Da / Density % sol: 45.1 %
Crystal growTemperature: 293 K / Method: batch mode / Details: PEG 6K, HEPES pH 7.0 / PH range: 7

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Data collection

DiffractionMean temperature: 293 K / Serial crystal experiment: N
Diffraction sourceSource: FREE ELECTRON LASER / Site: SwissFEL ARAMIS / Beamline: ESC / Wavelength: 1.03 Å
DetectorType: PSI JUNGFRAU 8M / Detector: PIXEL / Date: Jun 1, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 1.54→40 Å / Num. obs: 102828 / % possible obs: 100 % / Redundancy: 638 % / R split: 0.178 / Net I/σ(I): 5.6
Reflection shellResolution: 1.54→1.58 Å / Num. unique obs: 5104 / R split: 0.287

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Processing

Software
NameVersionClassification
REFMAC5.8.0430refinement
CrystFELdata scaling
CrystFELdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.54→37.2 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.956 / SU B: 1.499 / SU ML: 0.055 / Cross valid method: THROUGHOUT / ESU R: 0.078 / ESU R Free: 0.077 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19214 5282 5.1 %RANDOM
Rwork0.16752 ---
obs0.16883 97505 99.93 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 15.606 Å2
Baniso -1Baniso -2Baniso -3
1-1.03 Å2-0 Å2-0.96 Å2
2---0.59 Å20 Å2
3---0.08 Å2
Refinement stepCycle: 1 / Resolution: 1.54→37.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5578 0 0 696 6274
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0125807
X-RAY DIFFRACTIONr_bond_other_d0.0010.0165321
X-RAY DIFFRACTIONr_angle_refined_deg1.8521.8357936
X-RAY DIFFRACTIONr_angle_other_deg0.6441.77612178
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.565742
X-RAY DIFFRACTIONr_dihedral_angle_2_deg7.756560
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.83410820
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0940.2832
X-RAY DIFFRACTIONr_gen_planes_refined0.010.027263
X-RAY DIFFRACTIONr_gen_planes_other0.0050.021465
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.6051.5112926
X-RAY DIFFRACTIONr_mcbond_other1.6031.512925
X-RAY DIFFRACTIONr_mcangle_it2.3682.7073661
X-RAY DIFFRACTIONr_mcangle_other2.3692.7083662
X-RAY DIFFRACTIONr_scbond_it2.6291.7752881
X-RAY DIFFRACTIONr_scbond_other2.631.7762879
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.0623.1164268
X-RAY DIFFRACTIONr_long_range_B_refined5.82317.916537
X-RAY DIFFRACTIONr_long_range_B_other5.65816.776433
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.54→1.58 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.279 365 -
Rwork0.248 7207 -
obs--99.85 %

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