Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile pseudomonas aeruginosa
A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P212121. A complete data set to 2.1 Å resolution has been measured. The st...
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Published in | Protein science Vol. 6; no. 11; pp. 2462 - 2464 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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Cold Spring Harbor Laboratory Press
01.11.1997
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Abstract | A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P212121. A complete data set to 2.1 Å resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R‐factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an a‐amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme. |
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AbstractList | A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P2(1)2(1)2(1). A complete data set to 2.1 A resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R-factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an alpha-amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme. A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P212121. A complete data set to 2.1 Å resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R‐factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an a‐amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme. Abstract A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the presence of PEG 6000 at pH 7 and pH 8. They belong to the space group P2 1 2 1 2 1 . A complete data set to 2.1 Å resolution has been measured. The structure has been determined by the molecular replacement method using the coordinates of the mesophilic alkaline protease as a model. The molecular replacement solution displays a correlation coefficient of 0.39 and an R ‐factor of 0.48. Subsequent inspection of the electron density map in the active site region has confirmed the correctness of the solution. Model building and structure refinement will be initiated when the protease sequence becomes fully available. This is the second report, following one on an a‐amylase, of the preliminary crystallographic characterization of a psychrophilic enzyme. |
Author | Beeumen, Jozef Van Chessa, Jean‐Pierre Gerday, Charles Villeret, Vincent |
AuthorAffiliation | Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, Belgium |
AuthorAffiliation_xml | – name: Laboratorium voor Eiwitbiochemie en Eiwitengineering, Universiteit Gent, Belgium |
Author_xml | – sequence: 1 givenname: Vincent surname: Villeret fullname: Villeret, Vincent – sequence: 2 givenname: Jozef Van surname: Beeumen fullname: Beeumen, Jozef Van email: jozef.vanbeeumen@rug.ac.be – sequence: 3 givenname: Jean‐Pierre surname: Chessa fullname: Chessa, Jean‐Pierre – sequence: 4 givenname: Charles surname: Gerday fullname: Gerday, Charles |
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Snippet | A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained in the... Abstract A cold alkaline protease, isolated from an Antarctic Pseudomonas aeruginosa strain, has been purified and crystallized. Large crystals were obtained... |
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SubjectTerms | Antarctic Regions Bacterial Proteins - chemistry Calcium Cold Temperature Crystallography, X-Ray Metalloendopeptidases - chemistry Models, Molecular protease Pseudomonas aeruginosa - enzymology psychrophilic enzymes Sequence Homology, Amino Acid Serine Endopeptidases X‐ray crystallography Zinc |
Title | Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile pseudomonas aeruginosa |
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