![Data-processing statistics for P. horikoshii acylphos- phatase](https://journals.plos.org/plosbiology/article/figure/image?size=medium&id=10.1371/journal.pbio.1001027.t002)
A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.researchgate.net/profile/Mark-Allen-8/publication/7954977/figure/fig2/AS:672489109725199@1537345306890/Structure-of-the-L5-loop-of-AcP-is-not-conserved-Residues-involved-in-stabilizing-the_Q320.jpg)
PDF) Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshii Structural Insights into Enzymatic Catalysis, Thermostability, and Dimerization † , ‡
![Data-processing statistics for P. horikoshii acylphos- phatase](https://cdn.rcsb.org/images/structures/1w2i_model-1.jpeg)
RCSB PDB - 1W2I: Crystal structuore of acylphosphatase from Pyrococcus horikoshii complexed with formate
![Data-processing statistics for P. horikoshii acylphos- phatase](https://journals.plos.org/plosbiology/article/figure/image?size=medium&id=10.1371/journal.pbio.1001027.t001)
A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.brenda-enzymes.org/Mol/Mol.image.php?ID=27693&size=small)
Information on EC 1.13.11.12 - linoleate 13S-lipoxygenase - BRENDA Enzyme Database
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.science.org/cms/10.1126/science.aay2784/asset/6dc4c6dd-9e60-4348-bbf2-c7f2e4710b30/assets/graphic/371_aay2784_f2.jpeg)
Parallel molecular mechanisms for enzyme temperature adaptation
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.researchgate.net/profile/Chiara-Nediani/publication/12270267/figure/fig1/AS:277457543417856@1443162441277/Co-immunoprecipitation-of-SERCA-2-and-the-acylphosphatase-mutant-Asn41Ser-by-monoclonal_Q320.jpg)
Co-immunoprecipitation of SERCA2a and acylphosphatase (ACP) with
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.science.org/cms/10.1126/science.aay2784/asset/04825956-6c0a-419b-a24f-541471ddc44d/assets/graphic/371_aay2784_f6.jpeg)
Parallel molecular mechanisms for enzyme temperature adaptation
![Data-processing statistics for P. horikoshii acylphos- phatase](https://journals.plos.org/plosone/article/figure/image?size=medium&id=10.1371/journal.pone.0258821.g002)
Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.tandfonline.com/doi/cover-img/10.1080/imbc20.v024.i05-06)
Full article: Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review)
![Data-processing statistics for P. horikoshii acylphos- phatase](https://www.researchgate.net/publication/7954977/figure/tbl1/AS:672489113923588@1537345307238/Crystallographic-Data-and-Refinement-Statistics-diffraction-data-values-in-parentheses.png)
Crystallographic Data and Refinement Statistics diffraction data
![Data-processing statistics for P. horikoshii acylphos- phatase](https://journals.plos.org/plosbiology/article/figure/image?size=medium&id=10.1371/journal.pbio.1001027.g005)
A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity
![Data-processing statistics for P. horikoshii acylphos- phatase](https://callisto.ggsrv.com/imgsrv/FastFetch/UBER1/ZI-5AMJ-2011-MAR00-IDSI-190-1)
A rigidifying salt-bridge favors the activity of thermophilic enzyme at high temperatures at the expense of low-temperature activity - Document - Gale OneFile: Health and Medicine
![Data-processing statistics for P. horikoshii acylphos- phatase](https://files.rcsb.org/pub/pdb/validation_reports/w2/1w2i/1w2i_multipercentile_validation.png)
RCSB PDB - 1W2I: Crystal structuore of acylphosphatase from Pyrococcus horikoshii complexed with formate
![Data-processing statistics for P. horikoshii acylphos- phatase](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-020-79537-y/MediaObjects/41598_2020_79537_Fig5_HTML.png)
Crystal structure and DNA cleavage mechanism of the restriction DNA glycosylase R.CcoLI from Campylobacter coli