Show legend Show as text

Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_130648,IEDB_130701,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_137485,IEDB_1391961,IEDB_1394182,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_144990,IEDB_151528,IEDB_152206,IEDB_152214,IEDB_152215,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_885822,IEDB_983930,SB_154,SB_44,SB_67,SB_7,SB_72,SB_86

• Article ID: 1483
  Skurnik M "Molecular genetics, biochemistry and biological role of Yersinia lipopolysaccharide" - Book: The Genus Yersinia (series: Advances in Experimental Medicine and Biolog) (2003) 187-198
  

  Lipopolysaccharide (LPS) is the major component of the outer leaflet of the outer membrane of Gram-negative bacteria. The LPS molecule is composed of two biosynthetic entities: the lipid A--core and the O-polysaccharide (O-antigen). Most biological effects of LPS are due to the lipid A part, however, there is an increasing body of evidence also with Yersinia indicating that O-antigen plays an important role in effective colonization of host tissues, resistance to complement-mediated killing and in the resistance to cationic antimicrobial peptides that are key elements of the innate immune system. The biosynthesis of O-antigen requires numerous enzymatic activities and includes the biosynthesis of individual NDP-activated precursor sugars in the cytoplasm, linkage and sugar-specific transferases, O-unit flippase, O-antigen polymerase and O-chain length determinant. Based on this enzymatic mode of O-antigen biosynthesis LPS isolated from bacteria is a heterologous population of molecules; some do not carry any O-antigen while others that do have variation in the O-antigen chain lengths. The genes required for the O-antigen biosynthesis are located in O-antigen gene clusters that in genus Yersinia is located between the hemH and gsk genes. Temperature regulates the O-antigen expression in Y. enterocolitica and Y. pseudotuberculosis; bacteria grown at room temperature (RT, 22-25 degrees C) produce in abundance O-antigen while only trace amounts are present in bacteria grown at 37 degrees C. Even though the amount of O-antigen is known to fluctuate under different growth conditions in many bacteria very little detailed information is available on the control of the O-antigen biosynthetic machinery.

  Lipopolysaccharide, genetic, lipopolysaccharides, structure, core, genetics, role, strain, cell, molecular, biological, cell wall, biochemistry, PAGE, function, genus, bacteriophage, Yersinia, molecular genetics, Yersinia pestis, influence, Bacteriophages, growth, temperature

  NCBI PubMed ID: 12756756
  Publication DOI: 10.1007/0-306-48416-1_38
  Publisher: Springer US.
  Editors: Skurnik M, Bengoechea JA, Granfors K
  Institutions: Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Finland
  
   
  
  Yersinia enterocolitica O8
  CSDB ID 4911 (all data & tools)

Show legend Show as text

Structure type: monomer
Trivial name: main polar lipid (MPL), glycoglycerophospholipid
Compound class: glycolipid
Contained glycoepitopes: IEDB_130695

• Article ID: 1488
  Swain M, Brisson J, Sprott GD, Cooper FP, Patel GB "Identification of b-L-gulose as the sugar moiety of the main polar lipid Thermoplasma acidophilum" - Biochimica et Biophysica Acta 1345(1) (1997) 56-64
  

  The main polar lipid (MPL) of Thermoplasma acidophilum has been purified and its structure determined. NMR, mass spectrometry, and capillary gas chromatography-mass spectrometry experiments have shown that the previously unidentified sugar moiety of MPL is the rare sugar L-gulose. MPL is thus a tetraether lipid with cyclopentane rings and head groups of phosphoglycerol, as previously reported, and β-L-gulopyranose. Further, MPL is also the dominant lipid found in lipid extracts from another species of the Thermoplasma genus, T. volcanium, suggesting that L-gulose may represent a dominant sugar moiety of the polar lipids biosynthesized by this archaeobacterial genus. Minor phospholipids were tentatively identified as diether and hydroxydiether analogs of phosphatidylglycerol, and phosphatidylinositol.

  structure, lipid, sugar, gulose, main polar lipid, b-L-gulose, Thermoplasma acidophilum, Thermoplasma, tetraether lipid

  NCBI PubMed ID: 9084501
  Publication DOI: 10.1016/s0005-2760(96)00163-4
  Journal NLM ID: 0217513
  Publisher: Elsevier
  Correspondence: dennis.sprott@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council of Canada, 100 Sussex DriÍe, Ottawa, Ont. K1A 0R6 Canada
  Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, sugar analysis, TLC, ESI-MS, NMR-1D, extraction, CD
  
   
  
  Thermoplasma acidophilum
  CSDB ID 4980 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: bleomycin
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 4744
  Neese F, Zaleski JM, Loeb Zaleski K, Solomon EI "Electronic Structure of Activated Bleomycin: Oxygen Intermediates in Heme versus Non-Heme Iron" - Journal of the American Chemical Society 122 (2000) 11703-11724
  

  Bleomycin (BLM) is a glycopeptide antibiotic produced by the fungus Streptomyces verticillus which is used clinically for anticancer therapy. It is most active as an iron complex. A detailed spectroscopic and theoretical study of the ferric form of the drug, Fe(III)BLM, and its activated form, ABLM, is reported. ABLM, which has been shown to be a ferric hydroperoxide complex, is the last detectable intermediate in the reaction cycle of BLM that leads to a DNA radical and subsequent cleavage. Both forms of the drug are low-spin Fe(III) complexes and were studied with electron paramagnetic resonance (EPR), magnetic circular dichroism (MCD), and absorption (ABS) spectroscopy. In addition, resonance Raman (rR) and circular dichroism (CD) spectra are reported for Fe(III)BLM. The g matrix was analyzed in detail, and Griffith's model for low-spin d5 complexes was experimentally evaluated. A ligand field analysis of the d−d region of the optical spectra resulted in a complete determination of the ligand field parameters for both forms of the drug. Analysis of the optical and rR data led to assignment of the main ABS band at 386 nm in both Fe(III)BLM and ABLM as deprotonated amide-to-iron ligand-to-metal charge-transfer (LMCT) transitions. Revised vibrational assignments are proposed on the basis of B3LYP frequency calculations on models of Fe(III)BLM. On the basis of energetically optimized geometric models for Fe(III)BLM and ABLM the electronic structures of both forms were analyzed using density functional theory (DFT), ab initio Hartree−Fock, and INDO/S methods. Conjugation of the deprotonated amide and pyrimidine functionalities is not proposed to be a major factor in the BLM electronic structure. In agreement with experimental data the calculations show that the ligand fields of both Fe(III)BLM and ABLM are dominated by the deprotonated amide that also determines the orientation of the t2g hole, the orientation of the g matrix and Mössbauer quadrupole tensor. The main LMCT band was shown to be an amide π-LMCT band. The calculations were extended to study the reactivity of the drug toward DNA. The possibilities of (a) heterolytic cleavage of the O−O bond in ABLM to give Fe(V)BLMO and H2O, (b) homolytic cleavage to give Fe(IV)BLM=O and OH•, and (c) direct attack of the hydroperoxide of ABLM on DNA to give Fe(IV)BLM=O, water, and a DNA radical were evaluated. Importantly, heterolytic cleavage is strongly suggested to be energetically unfavorable because it leads to a product which is best described as [Fe(IV)O BLM•] with a high-energy hole localized on the deprotonated amide. Initial homolytic cleavage is also discarded on the basis of the specificity of the reaction; this leads to the new working hypothesis that ABLM chemistry proceeds by direct attack of the substrate C−H bond by the low-spin ferric hydroperoxide complex ABLM. The electronic structure contributions to such a reaction are discussed, and the relationship of ABLM and cytochrome P450 is addressed.

  Publication DOI: 10.1021/ja001812y
  Journal NLM ID: 7503056
  Publisher: American Chemical Society
  Institutions: Department of Chemistry, Stanford UniVersity, Stanford, California 94305-5080
  Methods: CD, EPR, MCD spectroscopy, ABS spectroscopy, RR spectroscopy, density functional calculations
  
   
  
  Streptomyces verticillus
  CSDB ID 40506 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: bleomycin A2
Compound class: glycoside
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5298
  Zhang N, Zhu X, Yang D, Cai J, Tao M, Wang L, Duan Y, Shen B, Xu Z "Improved production of the tallysomycin H-1 in Streptoalloteichus hindustanus SB8005 strain by fermentation optimization" - Applied Microbiology and Biotechnology 86(5) (2010) 1345-1353
  

  Tallysomycin (TLM) H-1, a novel TLM analog, is the major product isolated from Streptoalloteichus hindustanus SB8005, a genetically engineered strain from S. hindustanus E465-94 ATCC 31158. Based on the structural comparison and experimental assays, TLM H-1 represents a novel bleomycin (BLM) analog displaying DNA cleavage activity similar to its parent compounds TLM and BLM, both representatives of the glycopeptide anticancer antibiotics. The low titer of TLM H-1 in the engineered SB8005 strain has greatly limited its further study. In this paper, fermentation optimization for TLM H-1 production in the SB8005 strain is described; single-factor optimization and response surface methodology proved invaluable. The results indicated that three variables including distiller's grains and solubles, copper sulfate, and maltose out of eight parameters could significantly influence the TLM H-1 production. With systematic comparison and evaluation, the final optimized fermentation medium was determined. The optimized yield of TLM H-1 in the bench-top fermentor was 249.9 mg/L, which is 26.8 times higher than reported using the original medium, and 12.9-fold higher than that of the parent compound TLM produced by the wild-type strain. This work provides important parameters for TLM H-1 production by fermentation and should facilitate further mechanistic studies and clinical developments of TLM H-1 as an anticancer agent.

  response surface methodology, bleomycin, fermentation optimization, Plackett-Burman design, Streptoalloteichus hindustanus, tallysomycin

  NCBI PubMed ID: 20049429
  Publication DOI: 10.1007/s00253-009-2406-9
  Journal NLM ID: 8406612
  Publisher: Springer
  Correspondence: znxu@zju.edu.cn
  Institutions: Institute of Bioengineering, Department of Chemical and Biological Engineering, Zhejiang University, Zhejiang, China, Hunan Engineering Research Center of Combinatorial Biosynthesis and Natural Product Drug Discovery, Hunan, China, Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, USA
  Methods: HPLC, extraction, cell growth
  
   
  
  Streptomyces verticillus ATCC 15003
  CSDB ID 44399 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: tallysomycin A
Compound class: glycoside
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5298
  Zhang N, Zhu X, Yang D, Cai J, Tao M, Wang L, Duan Y, Shen B, Xu Z "Improved production of the tallysomycin H-1 in Streptoalloteichus hindustanus SB8005 strain by fermentation optimization" - Applied Microbiology and Biotechnology 86(5) (2010) 1345-1353
  

  Tallysomycin (TLM) H-1, a novel TLM analog, is the major product isolated from Streptoalloteichus hindustanus SB8005, a genetically engineered strain from S. hindustanus E465-94 ATCC 31158. Based on the structural comparison and experimental assays, TLM H-1 represents a novel bleomycin (BLM) analog displaying DNA cleavage activity similar to its parent compounds TLM and BLM, both representatives of the glycopeptide anticancer antibiotics. The low titer of TLM H-1 in the engineered SB8005 strain has greatly limited its further study. In this paper, fermentation optimization for TLM H-1 production in the SB8005 strain is described; single-factor optimization and response surface methodology proved invaluable. The results indicated that three variables including distiller's grains and solubles, copper sulfate, and maltose out of eight parameters could significantly influence the TLM H-1 production. With systematic comparison and evaluation, the final optimized fermentation medium was determined. The optimized yield of TLM H-1 in the bench-top fermentor was 249.9 mg/L, which is 26.8 times higher than reported using the original medium, and 12.9-fold higher than that of the parent compound TLM produced by the wild-type strain. This work provides important parameters for TLM H-1 production by fermentation and should facilitate further mechanistic studies and clinical developments of TLM H-1 as an anticancer agent.

  response surface methodology, bleomycin, fermentation optimization, Plackett-Burman design, Streptoalloteichus hindustanus, tallysomycin

  NCBI PubMed ID: 20049429
  Publication DOI: 10.1007/s00253-009-2406-9
  Journal NLM ID: 8406612
  Publisher: Springer
  Correspondence: znxu@zju.edu.cn
  Institutions: Institute of Bioengineering, Department of Chemical and Biological Engineering, Zhejiang University, Zhejiang, China, Hunan Engineering Research Center of Combinatorial Biosynthesis and Natural Product Drug Discovery, Hunan, China, Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, USA
  Methods: HPLC, extraction, cell growth
  
   
  
  Streptoalloteichus hindustanus E465-94 ATCC 31158
  CSDB ID 44400 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: tallysomycin H-1
Compound class: glycoside
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5298
  Zhang N, Zhu X, Yang D, Cai J, Tao M, Wang L, Duan Y, Shen B, Xu Z "Improved production of the tallysomycin H-1 in Streptoalloteichus hindustanus SB8005 strain by fermentation optimization" - Applied Microbiology and Biotechnology 86(5) (2010) 1345-1353
  

  Tallysomycin (TLM) H-1, a novel TLM analog, is the major product isolated from Streptoalloteichus hindustanus SB8005, a genetically engineered strain from S. hindustanus E465-94 ATCC 31158. Based on the structural comparison and experimental assays, TLM H-1 represents a novel bleomycin (BLM) analog displaying DNA cleavage activity similar to its parent compounds TLM and BLM, both representatives of the glycopeptide anticancer antibiotics. The low titer of TLM H-1 in the engineered SB8005 strain has greatly limited its further study. In this paper, fermentation optimization for TLM H-1 production in the SB8005 strain is described; single-factor optimization and response surface methodology proved invaluable. The results indicated that three variables including distiller's grains and solubles, copper sulfate, and maltose out of eight parameters could significantly influence the TLM H-1 production. With systematic comparison and evaluation, the final optimized fermentation medium was determined. The optimized yield of TLM H-1 in the bench-top fermentor was 249.9 mg/L, which is 26.8 times higher than reported using the original medium, and 12.9-fold higher than that of the parent compound TLM produced by the wild-type strain. This work provides important parameters for TLM H-1 production by fermentation and should facilitate further mechanistic studies and clinical developments of TLM H-1 as an anticancer agent.

  response surface methodology, bleomycin, fermentation optimization, Plackett-Burman design, Streptoalloteichus hindustanus, tallysomycin

  NCBI PubMed ID: 20049429
  Publication DOI: 10.1007/s00253-009-2406-9
  Journal NLM ID: 8406612
  Publisher: Springer
  Correspondence: znxu@zju.edu.cn
  Institutions: Institute of Bioengineering, Department of Chemical and Biological Engineering, Zhejiang University, Zhejiang, China, Hunan Engineering Research Center of Combinatorial Biosynthesis and Natural Product Drug Discovery, Hunan, China, Division of Pharmaceutical Sciences, School of Pharmacy, University of Wisconsin-Madison, Madison, USA
  Methods: HPLC, extraction, cell growth
  
   
  
  Streptoalloteichus hindustanus SB8005
  CSDB ID 44401 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: zeocin
Compound class: glycoside
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 5380
  Dragosits M, Yan S, Razzazi-Fazeli E, Wilson IB, Rendic D "Enzymatic properties and subtle differences in the substrate specificity of phylogenetically distinct invertebrate N-glycan processing hexosaminidases" - Glycobiology 25(4) (2015) 448-464
  

  Fused lobes (FDL) hexosaminidases are the most recently genetically defined glycosidases involved in the biosynthesis of N-glycans in invertebrates, and their narrow specificity is essential for the generation of paucimannosidic N-glycans in insects. In this study, we explored the potential of FDL hexosaminidases in the utilization of different artificial and natural substrates, both as purified, native compounds or generated in vitro using various relevant glycosyltransferases. In addition to the already-known FDL enzyme from Drosophila melanogaster, we now have identified and characterized the Apis mellifera FDL homolog. The enzymatic properties of the soluble forms of the affinity-purified insect FDL enzymes, expressed in both yeast and insect cells, were compared with those of the phylogenetically distinct recombinant Caenorhabditis elegans FDL-like enzymes and the N-acetylgalactosamine (GalNAc)-specific Caenorhabditis hexosaminidase HEX-4. In tests with a range of substrates, including natural N-glycans, we show that the invertebrate FDL(-like) enzymes are highly specific for N-acetylglucosamine attached to the α1,3-mannose, but under extreme conditions also remove other terminal GalNAc and N-acetylglucosamine residues. Recombinant FDL also proved useful in the analysis of complex mixtures of N-glycans originating from wild-type and mutant Caenorhabditis strains, thereby aiding isomeric definition of paucimannosidic and hybrid N-glycans in this organism. Furthermore, differences in activity and specificity were shown for two site-directed mutants of Drosophila FDL, compatible with the high structural similarity of chitinolytic and N-glycan degrading exohexosaminidases in insects. Our studies are another indication for the variety of structural and function aspects in the GH20 hexosaminidase family important for both catabolism and biosynthesis of glycoconjugates in eukaryotes.

  N-glycans, fused lobes, hexosaminidase, insect, invertebrate

  NCBI PubMed ID: 25488985
  Publication DOI: 10.1093/glycob/cwu132
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: Rendic D
  Institutions: Department of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria, VetCore Facility for Research, University of Veterinary Medicine, Vienna, Austria
  
   
  
  Streptoalloteichus hindustanus
  CSDB ID 46342 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: EPS, polysaccharide
Contained glycoepitopes: IEDB_136045,IEDB_140629,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_152214,IEDB_153543,IEDB_153755,IEDB_174333,IEDB_423115,IEDB_983931,SB_192,SB_86

• Article ID: 5638
  Ravenscroft N, Walker SG, Dutton GG, Smit J "Identification, isolation, and structural studies of extracellular polysaccharides produced by Caulobacter crescentus" - Journal of Bacteriology 173(18) (1991) 5677-5684
  

  Caulobacters are adherent prosthecate bacteria that are members of bacterial biofouling communities in many environments. Investigation of the cell surface carbohydrates produced by two strains of the freshwater Caulobacter crescentus, CB2A and CB15A, revealed a hitherto undetected extracellular polysaccharide (EPS) or capsule. Isolation and characterization of the EPS fractions showed that each strain produced a unique neutral EPS which could not be readily removed from the cell surface by washing. Monosaccharide analysis showed that the main CB2A EPS contained D-glucose, D-gulose, and D-fucose in a ratio of 3:1:1, whereas the CB15A EPS fraction contained D-galactose, D-glucose, D-mannose, and D-fucose in approximately equal amounts. Methylation analysis of the main CB2A EPS showed the presence of terminal glucose and gulose groups, 3-linked fucosyl, and two 3,4-linked glucosyl units, thus confirming the pentasaccharide repeating unit indicated by 1H nuclear magnetic resonance analysis. Similar studies of the CB15A EPS revealed a tetrasaccharide repeating unit consisting of terminal galactose, 4-linked fucosyl, 3-linked glucosyl, and 3,4-linked mannosyl residues. EPS was not detectable by thin-section electron microscopy techniques, including some methods designed to preserve or enhance capsules, nor was the EPS readily detected on the cell surface by scanning electron microscopy when conventional fixation techniques were used; however, a structure consistent with EPS was revealed when samples were prepared by cryofixation and freeze-substitution methods

  exopolysaccharides, gulose, Caulobacter crescentus

  NCBI PubMed ID: 1885545
  Publication DOI: 10.1128/jb.173.18.5677-5684.1991
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Institutions: Department of Chemistry, University of British Columbia, Vancouver, Canada, Department of Microbiology, University of British Columbia, Vancouver, Canada
  Methods: 1H NMR, methylation, periodate oxidation, GC-MS, acid hydrolysis, GC, Smith degradation, methanolysis, enzymatic digestion, colorimetry, acetylation, SEC, reduction, cell growth, dialysis, phenol-sulfuric acid assay, SEM, derivatization, evaporation, TEM, centrifugation
  
   
  
  Caulobacter crescentus CB2A
  CSDB ID 47871 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: EPS, polysaccharide
Contained glycoepitopes: IEDB_136045,IEDB_140629,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_152214,IEDB_153543,IEDB_153755,IEDB_174333,IEDB_423115,IEDB_983931,SB_192,SB_86

• Article ID: 5638
  Ravenscroft N, Walker SG, Dutton GG, Smit J "Identification, isolation, and structural studies of extracellular polysaccharides produced by Caulobacter crescentus" - Journal of Bacteriology 173(18) (1991) 5677-5684
  

  Caulobacters are adherent prosthecate bacteria that are members of bacterial biofouling communities in many environments. Investigation of the cell surface carbohydrates produced by two strains of the freshwater Caulobacter crescentus, CB2A and CB15A, revealed a hitherto undetected extracellular polysaccharide (EPS) or capsule. Isolation and characterization of the EPS fractions showed that each strain produced a unique neutral EPS which could not be readily removed from the cell surface by washing. Monosaccharide analysis showed that the main CB2A EPS contained D-glucose, D-gulose, and D-fucose in a ratio of 3:1:1, whereas the CB15A EPS fraction contained D-galactose, D-glucose, D-mannose, and D-fucose in approximately equal amounts. Methylation analysis of the main CB2A EPS showed the presence of terminal glucose and gulose groups, 3-linked fucosyl, and two 3,4-linked glucosyl units, thus confirming the pentasaccharide repeating unit indicated by 1H nuclear magnetic resonance analysis. Similar studies of the CB15A EPS revealed a tetrasaccharide repeating unit consisting of terminal galactose, 4-linked fucosyl, 3-linked glucosyl, and 3,4-linked mannosyl residues. EPS was not detectable by thin-section electron microscopy techniques, including some methods designed to preserve or enhance capsules, nor was the EPS readily detected on the cell surface by scanning electron microscopy when conventional fixation techniques were used; however, a structure consistent with EPS was revealed when samples were prepared by cryofixation and freeze-substitution methods

  exopolysaccharides, gulose, Caulobacter crescentus

  NCBI PubMed ID: 1885545
  Publication DOI: 10.1128/jb.173.18.5677-5684.1991
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Institutions: Department of Chemistry, University of British Columbia, Vancouver, Canada, Department of Microbiology, University of British Columbia, Vancouver, Canada
  Methods: 1H NMR, methylation, periodate oxidation, GC-MS, acid hydrolysis, GC, Smith degradation, methanolysis, enzymatic digestion, colorimetry, acetylation, SEC, reduction, cell growth, dialysis, phenol-sulfuric acid assay, SEM, derivatization, evaporation, TEM, centrifugation
  
   
  
  Caulobacter crescentus CB2A
  CSDB ID 47272 (all data & tools)