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- PDB-3flo: Crystal structure of the carboxyl-terminal domain of yeast DNA po... -

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Basic information

Entry
Database: PDB / ID: 3flo
TitleCrystal structure of the carboxyl-terminal domain of yeast DNA polymerase alpha in complex with its B subunit
Components
  • (DNA polymerase alpha catalytic subunit ...) x 2
  • DNA polymerase alpha subunit BDNA polymerase
KeywordsTRANSFERASE / Protein-protein complex / phosphoesterase fold / OB fold / Zinc-binding motif / DNA replication / Nucleus / Phosphoprotein / DNA-binding / DNA-directed DNA polymerase / Nucleotidyltransferase
Function / homology
Function and homology information


Inhibition of replication initiation of damaged DNA by RB1/E2F1 / DNA replication initiation / RNA-templated DNA biosynthetic process / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching / premeiotic DNA replication / alpha DNA polymerase:primase complex / Activation of the pre-replicative complex / lagging strand elongation ...Inhibition of replication initiation of damaged DNA by RB1/E2F1 / DNA replication initiation / RNA-templated DNA biosynthetic process / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching / premeiotic DNA replication / alpha DNA polymerase:primase complex / Activation of the pre-replicative complex / lagging strand elongation / mitotic DNA replication initiation / telomere capping / leading strand elongation / DNA synthesis involved in DNA repair / DNA biosynthetic process / DNA replication origin binding / DNA replication initiation / replication fork / double-strand break repair / single-stranded DNA binding / nuclear envelope / 4 iron, 4 sulfur cluster binding / DNA replication / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / nucleotide binding / chromatin binding / mitochondrion / DNA binding / metal ion binding / nucleus
Similarity search - Function
Purple Acid Phosphatase; chain A, domain 2 - #60 / DNA Polymerase alpha, zinc finger / Hypothetical protein af0941 / DNA polymerase alpha subunit B N-terminal / DNA polymerase alpha, subunit B, N-terminal / DNA polymerase alpha, subunit B / DNA polymerase alpha catalytic subunit, N-terminal domain / DNA polymerase alpha, zinc finger domain superfamily / DNA Polymerase alpha zinc finger / DNA polymerase alpha subunit p180 N terminal ...Purple Acid Phosphatase; chain A, domain 2 - #60 / DNA Polymerase alpha, zinc finger / Hypothetical protein af0941 / DNA polymerase alpha subunit B N-terminal / DNA polymerase alpha, subunit B, N-terminal / DNA polymerase alpha, subunit B / DNA polymerase alpha catalytic subunit, N-terminal domain / DNA polymerase alpha, zinc finger domain superfamily / DNA Polymerase alpha zinc finger / DNA polymerase alpha subunit p180 N terminal / Zinc finger, DNA-directed DNA polymerase, family B, alpha / DNA polymerase alpha catalytic subunit, catalytic domain / DNA polymerase alpha/delta/epsilon, subunit B / DNA polymerase alpha/epsilon subunit B / Purple Acid Phosphatase; chain A, domain 2 / DNA polymerase family B, thumb domain / DNA polymerase family B signature. / DNA-directed DNA polymerase, family B, conserved site / DNA polymerase family B / DNA polymerase family B, exonuclease domain / DNA-directed DNA polymerase, family B, exonuclease domain / DNA-directed DNA polymerase, family B, multifunctional domain / DNA polymerase, palm domain superfamily / DNA polymerase type-B family / DNA-directed DNA polymerase, family B / 4-Layer Sandwich / Ribonuclease H superfamily / Ribonuclease H-like superfamily / DNA/RNA polymerase superfamily / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
DNA polymerase alpha catalytic subunit A / DNA polymerase alpha subunit B
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.5 Å
AuthorsKlinge, S.N. / Pellegrini, L.
CitationJournal: EMBO J / Year: 2009
Title: 3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases.
Authors: Sebastian Klinge / Rafael Núñez-Ramírez / Oscar Llorca / Luca Pellegrini /
Abstract: Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. The conserved catalytic and regulatory B subunits associate in ...Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. The conserved catalytic and regulatory B subunits associate in a constitutive heterodimer that represents the functional core of all three replicative polymerases. Here, we combine X-ray crystallography and electron microscopy (EM) to describe subunit interaction and 3D architecture of heterodimeric yeast Pol alpha. The crystal structure of the C-terminal domain (CTD) of the catalytic subunit bound to the B subunit illustrates a conserved mechanism of accessory factor recruitment by replicative polymerases. The EM reconstructions of Pol alpha reveal a bilobal shape with separate catalytic and regulatory modules. Docking of the B-CTD complex in the EM reconstruction shows that the B subunit is tethered to the polymerase domain through a structured but flexible linker. Our combined findings provide a structural template for the common functional architecture of the three major replicative DNA polymerases.
History
DepositionDec 19, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jun 9, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 5, 2012Group: Derived calculations
Revision 1.3Mar 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_conn / struct_ncs_dom_lim / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA polymerase alpha subunit B
I: DNA polymerase alpha catalytic subunit A
B: DNA polymerase alpha catalytic subunit A
C: DNA polymerase alpha subunit B
J: DNA polymerase alpha catalytic subunit A
D: DNA polymerase alpha catalytic subunit A
E: DNA polymerase alpha subunit B
K: DNA polymerase alpha catalytic subunit A
F: DNA polymerase alpha catalytic subunit A
G: DNA polymerase alpha subunit B
L: DNA polymerase alpha catalytic subunit A
H: DNA polymerase alpha catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)311,63485
Polymers304,86612
Non-polymers6,76773
Water10,287571
1
A: DNA polymerase alpha subunit B
B: DNA polymerase alpha catalytic subunit A
K: DNA polymerase alpha catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,17324
Polymers76,2173
Non-polymers1,95621
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7590 Å2
ΔGint-248 kcal/mol
Surface area27630 Å2
2
C: DNA polymerase alpha subunit B
D: DNA polymerase alpha catalytic subunit A
L: DNA polymerase alpha catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,78820
Polymers76,2173
Non-polymers1,57217
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6960 Å2
ΔGint-196 kcal/mol
Surface area27940 Å2
3
I: DNA polymerase alpha catalytic subunit A
E: DNA polymerase alpha subunit B
F: DNA polymerase alpha catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,88421
Polymers76,2173
Non-polymers1,66818
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7150 Å2
ΔGint-209 kcal/mol
Surface area27880 Å2
4
J: DNA polymerase alpha catalytic subunit A
G: DNA polymerase alpha subunit B
H: DNA polymerase alpha catalytic subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,78820
Polymers76,2173
Non-polymers1,57217
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7150 Å2
ΔGint-214 kcal/mol
Surface area27600 Å2
Unit cell
Length a, b, c (Å)85.411, 142.633, 175.255
Angle α, β, γ (deg.)90.00, 102.33, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
31E
41G
12B
22D
32F
42H

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ARGARGSERSER2AA248 - 7053 - 460
211ARGARGSERSER2CD248 - 7053 - 460
311ARGARGSERSER2EG248 - 7053 - 460
411ARGARGSERSER2GJ248 - 7053 - 460
112ASPASPLYSLYS2BC1273 - 140711 - 145
212ASPASPLYSLYS2DF1273 - 140711 - 145
312ASPASPLYSLYS2FI1273 - 140711 - 145
412ASPASPLYSLYS2HL1273 - 140711 - 145
122LEULEUCYSCYS4BC1422 - 1452160 - 190
222LEULEUCYSCYS4DF1422 - 1452160 - 190
322LEULEUCYSCYS4FI1422 - 1452160 - 190
422LEULEUCYSCYS4HL1422 - 1452160 - 190

NCS ensembles :
ID
1
2

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Components

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Protein , 1 types, 4 molecules ACEG

#1: Protein
DNA polymerase alpha subunit B / DNA polymerase / DNA polymerase I subunit B / DNA polymerase alpha:primase complex p86 subunit / Pol alpha-primase ...DNA polymerase I subunit B / DNA polymerase alpha:primase complex p86 subunit / Pol alpha-primase complex p86 subunit / DNA polymerase-primase complex p74 subunit


Mass: 51962.004 Da / Num. of mol.: 4 / Fragment: UNP residues 246-705
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: POL12 / Plasmid: RSF1-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Rosetta2 / References: UniProt: P38121

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DNA polymerase alpha catalytic subunit ... , 2 types, 8 molecules IJKLBDFH

#2: Protein/peptide
DNA polymerase alpha catalytic subunit A


Mass: 273.330 Da / Num. of mol.: 4 / Fragment: N-terminal parts of chains B, D, F, H
Source method: isolated from a genetically manipulated source
Details: Co-expressed from the same plasmid as a protein complex
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: POL1, CDC17 / Plasmid: RSF1-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Rosetta2
#3: Protein
DNA polymerase alpha catalytic subunit A / DNA polymerase I subunit A / DNA polymerase alpha:primase complex p180 subunit / Pol alpha-primase ...DNA polymerase I subunit A / DNA polymerase alpha:primase complex p180 subunit / Pol alpha-primase complex p180 subunit / DNA polymerase-primase complex p180 subunit


Mass: 23981.221 Da / Num. of mol.: 4
Fragment: Cysteine-rich C-terminal domain, UNP residues 1263-1468
Source method: isolated from a genetically manipulated source
Details: Co-expressed from the same plasmid as a protein complex
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: POL1, CDC17 / Plasmid: RSF1-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)Rosetta2 / References: UniProt: P13382, DNA-directed DNA polymerase

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Non-polymers , 3 types, 644 molecules

#4: Chemical...
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 65 / Source method: obtained synthetically / Formula: SO4
#5: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 571 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsCHAIN I, J, K, L; THE ELECTRON DENSITY MAP WAS NOT SUFFICIENTLY CLEAR TO ASSIGN UNAMBIGUOUSLY THE ...CHAIN I, J, K, L; THE ELECTRON DENSITY MAP WAS NOT SUFFICIENTLY CLEAR TO ASSIGN UNAMBIGUOUSLY THE AMINO ACID SEQUENCE TO THE REGIONS OF CHAINS B, D, F AND H N-TERMINAL TO ASP1273. THE DEPOSITORS HAVE PARTIALLY MODELLED THIS EXTRA DENSITY AS ALANINE TRI-PEPTIDES, WITH ARBITRARY CHAIN IDENTITY I, J, K, L FOR THE N-TERMINAL REGIONS OF CHAINS B, D, F, H, RESPECTIVELY.

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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: 3.42 Å3/Da / Density % sol: 64.04 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 0.1M MES, 1.26M Ammonium Sulfate, 3mM TCEP, pH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.2852
DetectorType: ADSC Q315R / Detector: CCD / Date: Jun 16, 2007 / Details: silicon monochromator
RadiationMonochromator: silicon / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2852 Å / Relative weight: 1
ReflectionResolution: 2.5→31.9 Å / Num. all: 141597 / Num. obs: 141597 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.3 % / Biso Wilson estimate: 58.4 Å2 / Rmerge(I) obs: 0.102 / Rsym value: 0.102 / Net I/σ(I): 5.2
Reflection shellResolution: 2.5→2.64 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.652 / Mean I/σ(I) obs: 1.2 / Num. unique all: 20778 / Rsym value: 0.652 / % possible all: 99.7

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHENIXmodel building
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.5→31.9 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.941 / SU B: 14.378 / SU ML: 0.161 / Cross valid method: THROUGHOUT / ESU R: 0.307 / ESU R Free: 0.217 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS, ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS, ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS
RfactorNum. reflection% reflectionSelection details
Rfree0.218 7082 5 %RANDOM
Rwork0.191 ---
obs0.192 134185 99.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 43.61 Å2
Baniso -1Baniso -2Baniso -3
1-0.51 Å20 Å2-0.45 Å2
2---0.8 Å20 Å2
3---0.1 Å2
Refinement stepCycle: LAST / Resolution: 2.5→31.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19648 0 333 571 20552
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.02220479
X-RAY DIFFRACTIONr_bond_other_d0.0040.0213857
X-RAY DIFFRACTIONr_angle_refined_deg1.5451.98327801
X-RAY DIFFRACTIONr_angle_other_deg0.9763.00233816
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.32352474
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.13224.461964
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.726153494
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.35915119
X-RAY DIFFRACTIONr_chiral_restr0.090.23049
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0222413
X-RAY DIFFRACTIONr_gen_planes_other0.0020.024030
X-RAY DIFFRACTIONr_nbd_refined0.210.23969
X-RAY DIFFRACTIONr_nbd_other0.1990.214015
X-RAY DIFFRACTIONr_nbtor_refined0.1860.210040
X-RAY DIFFRACTIONr_nbtor_other0.090.211054
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1590.2790
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.1520.22
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1270.223
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2090.285
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1980.215
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9971.515896
X-RAY DIFFRACTIONr_mcbond_other0.1361.54934
X-RAY DIFFRACTIONr_mcangle_it1.154220190
X-RAY DIFFRACTIONr_scbond_it2.05639238
X-RAY DIFFRACTIONr_scangle_it2.7464.57611
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A2550tight positional0.060.05
12C2550tight positional0.050.05
13E2550tight positional0.050.05
14G2550tight positional0.050.05
21B798tight positional0.060.05
22D798tight positional0.040.05
23F798tight positional0.040.05
24H798tight positional0.040.05
11A3294medium positional0.490.5
12C3294medium positional0.460.5
13E3294medium positional0.520.5
14G3294medium positional0.50.5
21B1500medium positional0.420.5
22D1500medium positional0.40.5
23F1500medium positional0.470.5
24H1500medium positional0.420.5
11A2550tight thermal0.120.5
12C2550tight thermal0.10.5
13E2550tight thermal0.10.5
14G2550tight thermal0.110.5
21B798tight thermal0.120.5
22D798tight thermal0.070.5
23F798tight thermal0.080.5
24H798tight thermal0.090.5
11A3294medium thermal0.612
12C3294medium thermal0.522
13E3294medium thermal0.532
14G3294medium thermal0.582
21B1500medium thermal0.682
22D1500medium thermal0.432
23F1500medium thermal0.522
24H1500medium thermal0.462
LS refinement shellResolution: 2.5→2.56 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.365 470 -
Rwork0.313 9897 -
obs--99.78 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.3725-0.57640.8551.4763-0.29891.3813-0.12640.28220.0475-0.19680.0986-0.01360.11910.0320.0278-0.1725-0.0878-0.0106-0.1597-0.0273-0.351824.39579.952153.367
21.08370.56581.19991.71761.46982.93230.1385-0.0314-0.15870.279-0.0768-0.14680.385-0.2213-0.0617-0.0187-0.1374-0.0765-0.13310.0031-0.2962-5.84219.346112.4
34.1162.31441.39032.23990.67430.989-0.14330.00290.7069-0.08220.04650.7213-0.1419-0.14110.0967-0.1607-0.0414-0.033-0.10370.06930.120419.691129.723161.381
41.5777-0.76841.47951.2863-0.68612.13390.00290.20940.15520.0282-0.0326-0.088-0.14790.0810.0297-0.1736-0.057-0.0408-0.12080.0867-0.29711.2769.477107.749
51.84120.07271.0510.7344-0.32223.3804-0.2614-0.31490.2510.22670.12040.0153-0.2855-0.14860.141-0.04160.1542-0.0636-0.1205-0.0851-0.261922.13393.256184.661
61.41970.55971.35571.87982.32685.9625-0.25440.66070.0536-0.59120.3973-0.2727-0.78140.9231-0.14290.1822-0.32160.10110.2125-0.0614-0.104110.91133.00585.599
75.24652.61871.10352.26410.44131.3978-0.49681.412-0.823-0.59480.9081-0.5593-0.13130.5983-0.41120.0784-0.37450.10850.4691-0.34970.098444.447116.11142.12
84.0763-1.79392.63011.5286-1.33712.84820.1792-0.5325-0.60850.03090.29260.56760.1322-0.7753-0.4718-0.1163-0.0787-0.02360.13340.26650.0705-29.7255.289112.681
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A248 - 705
2X-RAY DIFFRACTION2C248 - 705
3X-RAY DIFFRACTION3E248 - 705
4X-RAY DIFFRACTION4G248 - 705
5X-RAY DIFFRACTION5B1273 - 1452
6X-RAY DIFFRACTION6D1273 - 1452
7X-RAY DIFFRACTION7F1273 - 1452
8X-RAY DIFFRACTION8H1273 - 1452

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