Novel bacterial clade reveals origin of form I Rubisco

Banda, Douglas M.; Pereira, Jose H.; Liu, Albert K.; Orr, Douglas J.; Hammel, Michal; He, Christine; Parry, Martin A. J.; Carmo-Silva, Elizabete; Adams, Paul D.; Banfield, Jillian F.; Shih, Patrick M.

doi:10.1038/s41477-020-00762-4

Title: Novel bacterial clade reveals origin of form I Rubisco

Journal Article · Mon Aug 31 00:00:00 UTC 2020 · Nature Plants (Online)

DOI: https://doi.org/10.1038/s41477-020-00762-4 · OSTI ID:1782186

^[1]; Pereira, Jose H. ^[2];

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^[3]; Hammel, Michal ^[4];

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^[3]; Adams, Paul D. ^[2];

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Univ. of California, Davis, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Joint BioEnergy Institute (JBEI), Emeryville, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Lancaster Univ. (United Kingdom)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Univ. of California, Berkeley, CA (United States)
Univ. of California, Berkeley, CA (United States); Chan Zuckerberg Biohub, San Francisco, CA (United States)
Univ. of California, Davis, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Joint BioEnergy Institute (JBEI), Emeryville, CA (United States)

Rubisco sustains the biosphere through the fixation of CO₂ into biomass. In plants and cyanobacteria, form I Rubisco is structurally comprised of large and small subunits, whereas all other Rubisco forms lack small subunits. The rise of the form I complex through the innovation of small subunits represents a key, yet poorly understood, transition in Rubisco's evolution. Here, through metagenomic analyses, we discovered a previously uncharacterized clade sister to form I Rubisco that evolved without small subunits. This clade diverged before the evolution of cyanobacteria and the origin of the small subunit; thus, it provides a unique reference point to advance our understanding of form I Rubisco evolution. Structural and kinetic data presented here reveal how a proto-form I Rubisco assembled and functioned without the structural stability imparted from small subunits. Our findings provide insight into a key evolutionary transition of the most abundant enzyme on Earth and the predominant entry point for nearly all global organic carbon.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); USDOE Bioenergy Research Centers (BRC) (United States). Joint BioEnergy Inst. (JBEI)

Sponsoring Organization:: Allen Foundation; Biotechnology and Biological Sciences Research Council (BBSRC); Camille and Henry Dreyfus Foundation; Chan Zuckerberg Biohub; Innovative Genomics Institute; National Institute of General Medical Sciences (NIGMS); USDOE Office of Science (SC); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1782186

Journal Information:: Nature Plants (Online), Journal Name: Nature Plants (Online) Journal Issue: 9 Vol. 6; ISSN 2055-0278

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

References (73)

Analysis of Protein Stability and Ligand Interactions by Thermal Shift Assay Huynh, Kathy; Partch, Carrie L. Current Protocols in Protein Science, Vol. 79, Issue 1 https://doi.org/10.1002/0471140864.ps2809s79	journal	February 2015
Microbial communities across a hillslope‐riparian transect shaped by proximity to the stream, groundwater table, and weathered bedrock Lavy, Adi; McGrath, David Geller; Matheus Carnevali, Paula B. Ecology and Evolution, Vol. 9, Issue 12 https://doi.org/10.1002/ece3.5254	journal	May 2019
Comparison of the crystal structures of L2 and L8S8 Rubisco suggests a functional role for the small subunit. Schneider, G.; Knight, S.; Andersson, I. The EMBO Journal, Vol. 9, Issue 7 https://doi.org/10.1002/j.1460-2075.1990.tb07371.x	journal	July 1990
UCSF Chimera?A visualization system for exploratory research and analysis Pettersen, Eric F.; Goddard, Thomas D.; Huang, Conrad C. Journal of Computational Chemistry, Vol. 25, Issue 13 https://doi.org/10.1002/jcc.20084	journal	January 2004
Crystal contacts as nature's docking solutions Krissinel, Evgeny Journal of Computational Chemistry, Vol. 31, Issue 1 https://doi.org/10.1002/jcc.21303	journal	January 2010
From chaperonins to Rubisco assembly and metabolic repair: Role of Chaperones in Rubisco Biogenesis Hayer-Hartl, Manajit Protein Science, Vol. 26, Issue 12 https://doi.org/10.1002/pro.3309	journal	October 2017
Comparative Protein Modelling by Satisfaction of Spatial Restraints Šali, Andrej; Blundell, Tom L. Journal of Molecular Biology, Vol. 234, Issue 3 https://doi.org/10.1006/jmbi.1993.1626	journal	December 1993
The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate Duff, Anthony P.; Andrews, T. John; Curmi, Paul M. G. Journal of Molecular Biology, Vol. 298, Issue 5 https://doi.org/10.1006/jmbi.2000.3724	journal	May 2000
High-Throughput SAXS for the Characterization of Biomolecules in Solution: A Practical Approach Dyer, Kevin N.; Hammel, Michal; Rambo, Robert P. Structural Genomics https://doi.org/10.1007/978-1-62703-691-7_18	book	October 2013
Green Bacteria: Insights into Green Bacterial Evolution through Genomic Analyses Bryant, Donald A.; Liu, Zhenfeng Advances in Botanical Research https://doi.org/10.1016/B978-0-12-397923-0.00004-7	book	December 2012
Role of the small subunit in ribulose-1,5-bisphosphate carboxylase/oxygenase Spreitzer, Robert J. Archives of Biochemistry and Biophysics, Vol. 414, Issue 2 https://doi.org/10.1016/S0003-9861(03)00171-1	journal	June 2003
Catalysis by cyanobacterial ribulose-bisphosphate carboxylase large subunits in the complete absence of small subunits. Andrews, T. J. Journal of Biological Chemistry, Vol. 263, Issue 25 https://doi.org/10.1016/S0021-9258(18)37741-X	journal	September 1988
Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2·4 Å resolution Knight, Stefan; Andersson, Inger; Brändén, Carl-Ivar Journal of Molecular Biology, Vol. 215, Issue 1 https://doi.org/10.1016/S0022-2836(05)80100-7	journal	September 1990
Accurate SAXS Profile Computation and its Assessment by Contrast Variation Experiments Schneidman-Duhovny, Dina; Hammel, Michal; Tainer, John A. Biophysical Journal, Vol. 105, Issue 4 https://doi.org/10.1016/j.bpj.2013.07.020	journal	August 2013
Structure and Function of RbcX, an Assembly Chaperone for Hexadecameric Rubisco Saschenbrecker, Sandra; Bracher, Andreas; Rao, Karnam Vasudeva Cell, Vol. 129, Issue 6 https://doi.org/10.1016/j.cell.2007.04.025	journal	June 2007
A new set of highly efficient, tag-cleaving proteases for purifying recombinant proteins Frey, Steffen; Görlich, Dirk Journal of Chromatography A, Vol. 1337 https://doi.org/10.1016/j.chroma.2014.02.029	journal	April 2014
A short history of RubisCO: the rise and fall (?) of Nature's predominant CO2 fixing enzyme Erb, Tobias J.; Zarzycki, Jan Current Opinion in Biotechnology, Vol. 49 https://doi.org/10.1016/j.copbio.2017.07.017	journal	February 2018
Inference of Macromolecular Assemblies from Crystalline State Krissinel, Evgeny; Henrick, Kim Journal of Molecular Biology, Vol. 372, Issue 3 https://doi.org/10.1016/j.jmb.2007.05.022	journal	September 2007
Subunit Interface Dynamics in Hexadecameric Rubisco van Lun, Michiel; van der Spoel, David; Andersson, Inger Journal of Molecular Biology, Vol. 411, Issue 5 https://doi.org/10.1016/j.jmb.2011.06.052	journal	September 2011
Prospects for improving CO2 fixation in C3-crops through understanding C4-Rubisco biogenesis and catalytic diversity Sharwood, Robert E.; Ghannoum, Oula; Whitney, Spencer M. Current Opinion in Plant Biology, Vol. 31 https://doi.org/10.1016/j.pbi.2016.04.002	journal	June 2016
Structure and function of Rubisco Andersson, Inger; Backlund, Anders Plant Physiology and Biochemistry, Vol. 46, Issue 3 https://doi.org/10.1016/j.plaphy.2008.01.001	journal	March 2008
Complex Chaperone Dependence of Rubisco Biogenesis Wilson, Robert H.; Hayer-Hartl, Manajit Biochemistry, Vol. 57, Issue 23 https://doi.org/10.1021/acs.biochem.8b00132	journal	March 2018
Revisiting Trade-offs between Rubisco Kinetic Parameters Flamholz, Avi I.; Prywes, Noam; Moran, Uri Biochemistry, Vol. 58, Issue 31 https://doi.org/10.1021/acs.biochem.9b00237	journal	July 2019
Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogs Pierce, John; Tolbert, N. E.; Barker, Robert Biochemistry, Vol. 19, Issue 5 https://doi.org/10.1021/bi00546a018	journal	March 1980
Mechanism of Rubisco: The Carbamate as General Base ^✗ Cleland, W. Wallace; Andrews, T. John; Gutteridge, Steven Chemical Reviews, Vol. 98, Issue 2 https://doi.org/10.1021/cr970010r	journal	April 1998
Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective Tabita, F. Robert Photosynthesis Research, Vol. 60, Issue 1, p. 1-28 https://doi.org/10.1023/A:1006211417981	journal	April 1999
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP Goloubinoff, Pierre; Christeller, John T.; Gatenby, Anthony A. Nature, Vol. 342, Issue 6252 https://doi.org/10.1038/342884a0	journal	December 1989
Coupled chaperone action in folding and assembly of hexadecameric Rubisco Liu, Cuimin; Young, Anna L.; Starling-Windhof, Amanda Nature, Vol. 463, Issue 7278 https://doi.org/10.1038/nature08651	journal	January 2010
Accurate assessment of mass, models and resolution by small-angle scattering Rambo, Robert P.; Tainer, John A. Nature, Vol. 496, Issue 7446 https://doi.org/10.1038/nature12070	journal	April 2013
Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS) Hura, Greg L.; Menon, Angeli L.; Hammel, Michal Nature Methods, Vol. 6, Issue 8 https://doi.org/10.1038/nmeth.1353	journal	July 2009
Missense meanderings in sequence space: a biophysical view of protein evolution DePristo, Mark A.; Weinreich, Daniel M.; Hartl, Daniel L. Nature Reviews Genetics, Vol. 6, Issue 9 https://doi.org/10.1038/nrg1672	journal	August 2005
Mediterranean grassland soil C–N compound turnover is dependent on rainfall and depth, and is mediated by genomically divergent microorganisms Diamond, Spencer; Andeer, Peter F.; Li, Zhou Nature Microbiology, Vol. 4, Issue 8 https://doi.org/10.1038/s41564-019-0449-y	journal	May 2019
Artificially evolved Synechococcus PCC6301 Rubisco variants exhibit improvements in folding and catalytic efficiency Greene, Dina N.; Whitney, Spencer M.; Matsumura, Ichiro Biochemical Journal, Vol. 404, Issue 3, p. 517-524 https://doi.org/10.1042/BJ20070071	journal	June 2007
Evolution and diversity of CO2 concentrating mechanisms in cyanobacteria Badger, Murray R.; Hanson, David; Price, G. Dean Functional Plant Biology, Vol. 29, Issue 3 https://doi.org/10.1071/PP01213	journal	January 2002
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized Tcherkez, G. G. B.; Farquhar, G. D.; Andrews, T. J. Proceedings of the National Academy of Sciences, Vol. 103, Issue 19 https://doi.org/10.1073/pnas.0600605103	journal	April 2006
Stability-activity tradeoffs constrain the adaptive evolution of RubisCO Studer, Romain A.; Christin, Pascal-Antoine; Williams, Mark A. Proceedings of the National Academy of Sciences, Vol. 111, Issue 6 https://doi.org/10.1073/pnas.1310811111	journal	January 2014
Evolution of the 3-hydroxypropionate bicycle and recent transfer of anoxygenic photosynthesis into the Chloroflexi Shih, Patrick M.; Ward, Lewis M.; Fischer, Woodward W. Proceedings of the National Academy of Sciences, Vol. 114, Issue 40 https://doi.org/10.1073/pnas.1710798114	journal	September 2017
Side Reactions Catalyzed by Ribulose-bisphosphate Carboxylase in the Presence and Absence of Small Subunits Morell, Matthew K.; Wilkin, Jean-Marc; Kane, Heather J. Journal of Biological Chemistry, Vol. 272, Issue 9 https://doi.org/10.1074/jbc.272.9.5445	journal	February 1997
Substrate-induced Assembly of Methanococcoides burtonii d-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Dimers into Decamers Alonso, Hernán; Blayney, Michelle J.; Beck, Jennifer L. Journal of Biological Chemistry, Vol. 284, Issue 49 https://doi.org/10.1074/jbc.M109.050989	journal	October 2009
Role of Small Subunit in Mediating Assembly of Red-type Form I Rubisco Joshi, Jidnyasa; Mueller-Cajar, Oliver; Tsai, Yi-Chin C. Journal of Biological Chemistry, Vol. 290, Issue 2 https://doi.org/10.1074/jbc.M114.613091	journal	November 2014
A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic Gunn, Laura H.; Valegård, Karin; Andersson, Inger Journal of Biological Chemistry, Vol. 292, Issue 16 https://doi.org/10.1074/jbc.M116.767145	journal	April 2017
MAFFT online service: multiple sequence alignment, interactive sequence choice and visualization Katoh, Kazutaka; Rozewicki, John; Yamada, Kazunori D. Briefings in Bioinformatics, Vol. 20, Issue 4 https://doi.org/10.1093/bib/bbx108	journal	September 2017
Variation in the Specificity Factor of C ₃ Higher Plant Rubiscos Determined by the Total Consumption of Ribulose-P ₂ Parry, M. A. J.; Keys, A. J.; Gutteridge, S. Journal of Experimental Botany, Vol. 40, Issue 3 https://doi.org/10.1093/jxb/40.3.317	journal	January 1989
Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships Tabita, F. R.; Satagopan, S.; Hanson, T. E. Journal of Experimental Botany, Vol. 59, Issue 7 https://doi.org/10.1093/jxb/erm361	journal	June 2007
Rubisco catalytic properties of wild and domesticated relatives provide scope for improving wheat photosynthesis Prins, Anneke; Orr, Douglas J.; Andralojc, P. John Journal of Experimental Botany, Vol. 67, Issue 6 https://doi.org/10.1093/jxb/erv574	journal	January 2016
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids Davis, I. W.; Leaver-Fay, A.; Chen, V. B. Nucleic Acids Research, Vol. 35, Issue Web Server https://doi.org/10.1093/nar/gkm216	journal	May 2007
PROMALS3D: a tool for multiple protein sequence and structure alignments Pei, Jimin; Kim, Bong-Hyun; Grishin, Nick V. Nucleic Acids Research, Vol. 36, Issue 7 https://doi.org/10.1093/nar/gkn072	journal	February 2008
FoXS: a web server for rapid computation and fitting of SAXS profiles Schneidman-Duhovny, D.; Hammel, M.; Sali, A. Nucleic Acids Research, Vol. 38, Issue Web Server https://doi.org/10.1093/nar/gkq461	journal	May 2010
Potent Inhibition of Ribulose-Bisphosphate Carboxylase by an Oxidized Impurity in Ribulose-1,5-Bisphosphate1 Kane, Heather J.; Wilkin, Jean-Marc; Portis, Archie R. Plant Physiology, Vol. 117, Issue 3 https://doi.org/10.1104/pp.117.3.1059	journal	July 1998
The Gene for the Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) Small Subunit Relocated to the Plastid Genome of Tobacco Directs the Synthesis of Small Subunits That Assemble into Rubisco Whitney, Spencer M.; Andrews, T. John The Plant Cell, Vol. 13, Issue 1 https://doi.org/10.1105/tpc.13.1.193	journal	January 2001
Phaser crystallographic software McCoy, Airlie J.; Grosse-Kunstleve, Ralf W.; Adams, Paul D. Journal of Applied Crystallography, Vol. 40, Issue 4 https://doi.org/10.1107/S0021889807021206	journal	July 2007
A graphical user interface to the CCP 4 program suite Potterton, Elizabeth; Briggs, Peter; Turkenburg, Maria Acta Crystallographica Section D Biological Crystallography, Vol. 59, Issue 7 https://doi.org/10.1107/S0907444903008126	journal	June 2003
Coot model-building tools for molecular graphics Emsley, Paul; Cowtan, Kevin Acta Crystallographica Section D Biological Crystallography, Vol. 60, Issue 12, p. 2126-2132 https://doi.org/10.1107/S0907444904019158	journal	November 2004
PHENIX: a comprehensive Python-based system for macromolecular structure solution Adams, Paul D.; Afonine, Pavel V.; Bunkóczi, Gábor Acta Crystallographica Section D Biological Crystallography, Vol. 66, Issue 2, p. 213-221 https://doi.org/10.1107/S0907444909052925	journal	January 2010
Towards automated crystallographic structure refinement with phenix.refine Afonine, Pavel V.; Grosse-Kunstleve, Ralf W.; Echols, Nathaniel Acta Crystallographica Section D Biological Crystallography, Vol. 68, Issue 4 https://doi.org/10.1107/S0907444912001308	journal	March 2012
Decision making in xia 2 Winter, Graeme; Lobley, Carina M. C.; Prince, Stephen M. Acta Crystallographica Section D Biological Crystallography, Vol. 69, Issue 7 https://doi.org/10.1107/S0907444913015308	journal	June 2013
Structure determination and refinement of ribulose 1,5-bisphosphate carboxylase/oxygenase from Synechococcus PCC6301 Newman, J.; Brändén, C. -I.; Jones, T. A. Acta Crystallographica Section D Biological Crystallography, Vol. 49, Issue 6 https://doi.org/10.1107/S090744499300530X	journal	November 1993
Berkeley Screen: a set of 96 solutions for general macromolecular crystallization Pereira, Jose H.; McAndrew, Ryan P.; Tomaleri, Giovani P. Journal of Applied Crystallography, Vol. 50, Issue 5 https://doi.org/10.1107/S1600576717011347	journal	September 2017
The age of Rubisco: the evolution of oxygenic photosynthesis Nisbet, E. G.; Grassineau, N. V.; Howe, C. J. Geobiology, Vol. 5, Issue 4 https://doi.org/10.1111/j.1472-4669.2007.00127.x	journal	December 2007
Organization and regulation of cbb CO2 assimilation genes in autotrophic bacteria Kusian, Bernhard; Bowien, Botho FEMS Microbiology Reviews, Vol. 21, Issue 2 https://doi.org/10.1111/j.1574-6976.1997.tb00348.x	journal	September 1997
A reversible decrease in ribulose 1,5-bisphosphate carboxylase/oxygenase carboxylation activity caused by the aggregation of the enzyme's large subunit is triggered in response to the exposure of moderate irradiance-grown plants to low irradiance Grabsztunowicz, Magda; Górski, Zbigniew; Luciński, Robert Physiologia Plantarum, Vol. 154, Issue 4 https://doi.org/10.1111/ppl.12322	journal	February 2015
Protein Dynamism and Evolvability Tokuriki, N.; Tawfik, D. S. Science, Vol. 324, Issue 5924 https://doi.org/10.1126/science.1169375	journal	April 2009
Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2 Aigner, H.; Wilson, R. H.; Bracher, A. Science, Vol. 358, Issue 6368 https://doi.org/10.1126/science.aap9221	journal	December 2017
Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs Tabita, F. R.; Hanson, T. E.; Li, H. Microbiology and Molecular Biology Reviews, Vol. 71, Issue 4 https://doi.org/10.1128/MMBR.00015-07	journal	December 2007
Draft Genome Sequence of Ornatilinea apprima P3M-1, an Anaerobic Member of the Chloroflexi Class Anaerolineae Hemp, James; Ward, Lewis M.; Pace, Laura A. Genome Announcements, Vol. 3, Issue 6 https://doi.org/10.1128/genomeA.01353-15	journal	November 2015
Draft Genome Sequence of Leptolinea tardivitalis YMTK-2, a Mesophilic Anaerobe from the Chloroflexi Class Anaerolineae Ward, Lewis M.; Hemp, James; Pace, Laura A. Genome Announcements, Vol. 3, Issue 6 https://doi.org/10.1128/genomeA.01356-15	journal	November 2015
Evolution of Oxygenic Photosynthesis Fischer, Woodward W.; Hemp, James; Johnson, Jena E. Annual Review of Earth and Planetary Sciences, Vol. 44, Issue 1 https://doi.org/10.1146/annurev-earth-060313-054810	journal	June 2016
Efficient protein alignment algorithm for protein search Lu, Zaixin; Zhao, Zhiyu; Fu, Bin BMC Bioinformatics, Vol. 11, Issue Suppl 1 https://doi.org/10.1186/1471-2105-11-S1-S34	journal	January 2010
Cultivation of Uncultured Chloroflexi Subphyla: Significance and Ecophysiology of Formerly Uncultured Chloroflexi 'Subphylum I' with Natural and Biotechnological Relevance Yamada, Takeshi; Sekiguchi, Yuji Microbes and Environments, Vol. 24, Issue 3 https://doi.org/10.1264/jsme2.ME09151S	journal	January 2009
How Protein Stability and New Functions Trade Off Tokuriki, Nobuhiko; Stricher, Francois; Serrano, Luis PLoS Computational Biology, Vol. 4, Issue 2 https://doi.org/10.1371/journal.pcbi.1000002	journal	February 2008
Evolution of Phototrophy in the Chloroflexi Phylum Driven by Horizontal Gene Transfer Ward, Lewis M.; Hemp, James; Shih, Patrick M. Frontiers in Microbiology, Vol. 9 https://doi.org/10.3389/fmicb.2018.00260	journal	February 2018
Directed Evolution of an Improved Rubisco; In Vitro Analyses to Decipher Fact from Fiction Zhou, Yu; Whitney, Spencer International Journal of Molecular Sciences, Vol. 20, Issue 20 https://doi.org/10.3390/ijms20205019	journal	October 2019
Structural basis for AcrVA4 inhibition of specific CRISPR-Cas12a Knott, Gavin J.; Cress, Brady F.; Liu, Jun-Jie eLife, Vol. 8 https://doi.org/10.7554/eLife.49110	journal	August 2019

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Additional file 1 of Discovery of a readily heterologously expressed Rubisco from the deep sea with potential for CO2 capture Zhang, Junli; Liu, Guoxia; Carvajal, Alonso I. figshare https://doi.org/10.6084/m9.figshare.16584425	dataset	January 2021

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Biogeochemistry
Evolution
Rubisco
SAXS
X-ray crystallography

Title: Novel bacterial clade reveals origin of form I Rubisco

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