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- PDB-3puv: Crystal Structure of an outward-facing MBP-Maltose transporter co... -

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Basic information

Entry
Database: PDB / ID: 3puv
TitleCrystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-VO4
Components
  • (Maltose transport system permease protein ...) x 2
  • Maltose-binding periplasmic protein
  • Maltose/maltodextrin import ATP-binding protein MalK
KeywordsHYDROLASE/TRANSPORT PROTEIN / ATP Binding Cassette / Nucleotide Binding Domain / Substrate Binding Protein / ABC Transporter / importer / ATPase / ATP binding / Maltodextrin binding / transmembrane integral membrane / HYDROLASE-TRANSPORT PROTEIN complex
Function / homology
Function and homology information


ABC-type maltose transporter / ABC-type maltose transporter activity / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / detection of maltose stimulus / maltose transport complex / maltose binding / carbohydrate transport / maltose transport ...ABC-type maltose transporter / ABC-type maltose transporter activity / negative regulation of maltose transport / enzyme IIA-maltose transporter complex / negative regulation of transmembrane transport / detection of maltose stimulus / maltose transport complex / maltose binding / carbohydrate transport / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / DNA-binding transcription factor binding / periplasmic space / DNA damage response / ATP hydrolysis activity / ATP binding / membrane / plasma membrane
Similarity search - Function
MalF N-terminal region-like / Periplasmic binding protein-like II / D-maltodextrin-binding protein, MBP / MalF N-terminal region-like / MalF N-terminal region-like / Maltose transport system permease protein MalF, P2 domain / MalF, N-terminal / : / : / Maltose transport system permease protein MalF P2 domain ...MalF N-terminal region-like / Periplasmic binding protein-like II / D-maltodextrin-binding protein, MBP / MalF N-terminal region-like / MalF N-terminal region-like / Maltose transport system permease protein MalF, P2 domain / MalF, N-terminal / : / : / Maltose transport system permease protein MalF P2 domain / MalF, N-terminal region, transmembrane helices / MetI-like fold / MetI-like / Maltose/Maltodextrin import ATP-binding protein malK family profile. / Transport-associated OB, type 2 / TOBE domain / : / MalK OB fold domain / ABC transporter, maltose/maltodextrin import, MalK-like / : / Molybdate/tungstate binding, C-terminal / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Nucleic acid-binding proteins / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Periplasmic binding protein-like II / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / D-Maltodextrin-Binding Protein; domain 2 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / Roll / Up-down Bundle / Beta Barrel / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
alpha-maltose / ADENOSINE-5'-DIPHOSPHATE / Chem-PGV / VANADATE ION / Maltose/maltodextrin transport system permease protein MalF / Maltose/maltodextrin-binding periplasmic protein / Maltose/maltodextrin transport system permease protein MalG / Maltose/maltodextrin import ATP-binding protein MalK
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsOldham, M.L. / Chen, J.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2011
Title: Snapshots of the maltose transporter during ATP hydrolysis.
Authors: Oldham, M.L. / Chen, J.
History
DepositionDec 6, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 10, 2011Provider: repository / Type: Initial release
Revision 1.1Sep 28, 2011Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
E: Maltose-binding periplasmic protein
F: Maltose transport system permease protein malF
G: Maltose transport system permease protein malG
A: Maltose/maltodextrin import ATP-binding protein MalK
B: Maltose/maltodextrin import ATP-binding protein MalK
hetero molecules


Theoretical massNumber of molelcules
Total (without water)224,75223
Polymers215,2905
Non-polymers9,46218
Water3,243180
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area34960 Å2
ΔGint-299 kcal/mol
Surface area76190 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.786, 97.125, 112.791
Angle α, β, γ (deg.)85.58, 78.71, 72.69
Int Tables number1
Space group name H-MP1

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Components

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Protein , 2 types, 3 molecules EAB

#1: Protein Maltose-binding periplasmic protein / MMBP / Maltodextrin-binding protein


Mass: 41622.047 Da / Num. of mol.: 1 / Fragment: unp residues 27-396
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b4034, ECDH10B_4223, JW3994, malE / Plasmid: pJF2 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AEX9
#4: Protein Maltose/maltodextrin import ATP-binding protein MalK


Mass: 42184.535 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b4035, ECDH10B_4224, JW3995, malK / Plasmid: pKJ / Production host: Escherichia coli (E. coli) / References: UniProt: P68187, EC: 3.6.3.19

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Maltose transport system permease protein ... , 2 types, 2 molecules FG

#2: Protein Maltose transport system permease protein malF


Mass: 57052.898 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b4033, ECDH10B_4222, JW3993, malF / Plasmid: pFG23 / Production host: Escherichia coli (E. coli) / References: UniProt: P02916
#3: Protein Maltose transport system permease protein malG


Mass: 32246.227 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b4032, ECDH10B_4221, JW3992, malG / Plasmid: pFG23 / Production host: Escherichia coli (E. coli) / References: UniProt: P68183

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Sugars , 1 types, 1 molecules

#5: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 6 types, 197 molecules

#6: Chemical
ChemComp-PGV / (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / PHOSPHATIDYLGLYCEROL / 2-VACCENOYL-1-PALMITOYL-SN-GLYCEROL-3-PHOSPHOGLYCEROL


Mass: 749.007 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C40H77O10P / Comment: phospholipid*YM
#7: Chemical ChemComp-UMQ / UNDECYL-MALTOSIDE / UNDECYL-BETA-D-MALTOPYRANOSIDE


Mass: 496.589 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C23H44O11 / Comment: detergent*YM
#8: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#9: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#10: Chemical ChemComp-VO4 / VANADATE ION


Mass: 114.939 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: VO4
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 180 / Source method: isolated from a natural source / Formula: H2O

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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: 3.9 Å3/Da / Density % sol: 68.42 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 27% PEG 400, 0.1M HEPES, 10 mM magnesium chloride, 50 mM sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K, pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.97965 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: May 10, 2009
RadiationMonochromator: double crystal monochromator and vertically focusing mirror
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97965 Å / Relative weight: 1
ReflectionResolution: 2.3→20 Å / Num. all: 77414 / Num. obs: 77414 / % possible obs: 58.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.071
Reflection shellResolution: 2.3→2.38 Å / Redundancy: 2.1 % / Mean I/σ(I) obs: 2.1 / Rsym value: 0.483 / % possible all: 14.7

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
REFMAC5.5.0088refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 2R6G

2r6g


Resolution: 2.4→20 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.893 / SU B: 24.152 / SU ML: 0.236 / Cross valid method: THROUGHOUT / ESU R: 0.619 / ESU R Free: 0.321 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25335 4002 5 %RANDOM
Rwork0.22278 ---
obs0.2243 76178 63.22 %-
all-77414 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 59.706 Å2
Baniso -1Baniso -2Baniso -3
1--1.52 Å2-1.8 Å2-0.67 Å2
2--1.13 Å21.29 Å2
3---1.52 Å2
Refinement stepCycle: LAST / Resolution: 2.4→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14602 0 262 180 15044
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.02215234
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.9364.88420678
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.23751885
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.82424.226627
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.226152513
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.3481579
X-RAY DIFFRACTIONr_chiral_restr0.0590.22362
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02111282
X-RAY DIFFRACTIONr_gen_planes_other
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_it0.1821.59380
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.345215120
X-RAY DIFFRACTIONr_scbond_it0.42135854
X-RAY DIFFRACTIONr_scangle_it0.7234.55557
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.4→2.461 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.315 68 -
Rwork0.284 1217 -
obs--13.89 %
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)
18.8942-1.8804-0.04927.2231.65176.59530.06560.4969-0.3610.4503-0.21830.8651.1021-0.46640.15270.7254-0.16070.17890.2640.00170.155-22.451-10.40117.164
21.28620.02480.82954.70581.88464.2789-0.0729-0.2458-0.08190.73640.06170.31420.9244-0.3180.01120.47880.06450.08380.19310.03140.0649-15.196-1.70921.739
30.91340.7823-1.44513.50.71894.0879-0.11-0.3854-0.08570.54210.3409-0.90040.70630.9482-0.23090.46880.2268-0.09350.4325-0.15470.39111.0523.5421
41.45540.00040.07656.52374.15935.02240.18640.1847-0.2209-0.481-0.20690.21990.2674-0.27360.02050.68190.09880.01470.0811-0.02920.0796-14.23-17.067-6.946
54.04652.9939-0.34297.7244-1.07235.59170.07250.5629-0.1614-1.51750.1172-0.46640.48880.4537-0.18971.42840.2160.23130.2813-0.13650.1786-7.119-11.572-16.527
613.37280.3202-0.78616.8527-1.80126.24640.2099-0.53361.1330.0823-0.0195-0.7638-0.19371.1064-0.19040.8635-0.01710.46270.2321-0.04920.65984.95927.653-0.896
73.6959-0.6578-1.12594.16630.67793.00340.21460.34760.402-0.9855-0.052-0.3204-0.3982-0.1065-0.16250.62450.06570.14390.14210.02620.0789-9.89517.159-2.367
84.89393.1699-0.95495.99-1.78921.58520.1550.2459-0.5932-0.7197-0.1445-1.93960.46391.0121-0.01050.92470.37080.43681.0111-0.3021.331419.255-4.69-4.409
91.32350.0901-0.67543.7149-0.29224.147-0.0454-0.0667-0.09930.3467-0.18490.2583-0.2938-0.56670.23030.4990.1366-0.0460.3094-0.22580.2151-43.91353.61868.525
103.69890.1059-0.75713.36510.32184.0048-0.11620.33520.3372-0.2542-0.10170.5779-1.3114-1.01210.21791.16410.6624-0.22410.4794-0.15250.3338-51.38672.78444.61
110.9481-0.2566-0.18332.16330.24623.15210.15060.07170.08670.0573-0.25830.2522-1.1283-0.71550.10770.80220.3531-0.07760.3314-0.2040.2202-47.20765.16457.358
1217.5817-6.2721-3.138110.15013.690610.9532-1.1475-1.7088-0.11162.30810.88490.69911.9630.4730.26261.43590.14250.41150.35370.00520.1335-30.29311.2560.345
130.6241-0.6922-1.33081.72981.61134.2563-0.22420.2445-0.2840.7243-0.43720.61520.6419-0.98250.66130.6081-0.18560.20960.3224-0.25210.3425-52.27637.91874.932
141.241-1.1622-1.13012.62571.49093.20250.06670.2909-0.0338-0.4634-0.3990.111-0.4324-0.61420.33230.41780.1667-0.12060.2756-0.11870.1198-36.69443.02727.904
151.0179-0.67-0.35853.45791.03763.68260.14160.02750.1225-0.1083-0.2436-0.096-0.463-0.03190.1020.17560.0486-0.00420.145-0.07620.2059-25.23144.14341.128
161.179-1.4758-1.02874.00282.74173.7417-0.0328-0.04410.0510.1033-0.0388-0.06760.17920.02210.07160.1980.0082-0.04610.1528-0.02080.1637-23.02531.83441.825
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 29
2X-RAY DIFFRACTION2A30 - 94
3X-RAY DIFFRACTION2A1501
4X-RAY DIFFRACTION2A2501
5X-RAY DIFFRACTION2A3001
6X-RAY DIFFRACTION2A382 - 383
7X-RAY DIFFRACTION3A95 - 188
8X-RAY DIFFRACTION4A189 - 289
9X-RAY DIFFRACTION5A290 - 372
10X-RAY DIFFRACTION6B2 - 29
11X-RAY DIFFRACTION7B30 - 228
12X-RAY DIFFRACTION7B3002
13X-RAY DIFFRACTION7B2502
14X-RAY DIFFRACTION7B1502
15X-RAY DIFFRACTION7B382 - 383
16X-RAY DIFFRACTION8B229 - 369
17X-RAY DIFFRACTION9E1 - 118
18X-RAY DIFFRACTION10E119 - 218
19X-RAY DIFFRACTION11E219 - 374
20X-RAY DIFFRACTION11F5004
21X-RAY DIFFRACTION12F10 - 53
22X-RAY DIFFRACTION13F54 - 274
23X-RAY DIFFRACTION14F275 - 503
24X-RAY DIFFRACTION14F2000
25X-RAY DIFFRACTION14F4001
26X-RAY DIFFRACTION14F4010
27X-RAY DIFFRACTION15G9 - 145
28X-RAY DIFFRACTION16G146 - 296
29X-RAY DIFFRACTION16G4003 - 4009
30X-RAY DIFFRACTION16F4002 - 4008

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