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Cloning, purification, crystallization and preliminary X-ray diffraction analysis of nitrile hydratase from the themophilic Bacillus smithii SC-J05-1
Nitrile hydratase (NHase) converts nitriles to the corresponding amides and is recognized as having important industrial applications. Purification, cloning, crystallization and initial crystallographic studies of the NHase from Bacillus smithii SC‐J05‐1 (Bs NHase) were conducted to analyze the acti...
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| Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-11, Vol.61 (11), p.974-977 |
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| container_issue | 11 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
| container_volume | 61 |
| creator | Hourai, Shinji Ishii, Takeshi Miki, Misao Takashima, Yoshiki Mitsuda, Satoshi Yanagi, Kazunori |
| description | Nitrile hydratase (NHase) converts nitriles to the corresponding amides and is recognized as having important industrial applications. Purification, cloning, crystallization and initial crystallographic studies of the NHase from Bacillus smithii SC‐J05‐1 (Bs NHase) were conducted to analyze the activity, specificity and thermal stability of this hydrolytic enzyme. Bs NHase was purified to homogeneity from microbial cells of B. smithii SC‐J05‐1 and the nucleotide sequences of both the α‐ and β‐subunits were determined. Purified Bs NHase was used for crystallization and several crystal forms were obtained by the vapour‐diffusion method. Microseeding and the addition of magnesium ions were essential components to obtain crystals suitable for X‐ray diffraction analysis. |
| doi_str_mv | 10.1107/S1744309105030939 |
| format | article |
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Purification, cloning, crystallization and initial crystallographic studies of the NHase from Bacillus smithii SC‐J05‐1 (Bs NHase) were conducted to analyze the activity, specificity and thermal stability of this hydrolytic enzyme. Bs NHase was purified to homogeneity from microbial cells of B. smithii SC‐J05‐1 and the nucleotide sequences of both the α‐ and β‐subunits were determined. Purified Bs NHase was used for crystallization and several crystal forms were obtained by the vapour‐diffusion method. 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Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>Nitrile hydratase (NHase) converts nitriles to the corresponding amides and is recognized as having important industrial applications. Purification, cloning, crystallization and initial crystallographic studies of the NHase from Bacillus smithii SC‐J05‐1 (Bs NHase) were conducted to analyze the activity, specificity and thermal stability of this hydrolytic enzyme. Bs NHase was purified to homogeneity from microbial cells of B. smithii SC‐J05‐1 and the nucleotide sequences of both the α‐ and β‐subunits were determined. Purified Bs NHase was used for crystallization and several crystal forms were obtained by the vapour‐diffusion method. Microseeding and the addition of magnesium ions were essential components to obtain crystals suitable for X‐ray diffraction analysis.</description><subject>Bacillus - enzymology</subject><subject>Bacillus smithii</subject><subject>Chromatography</subject><subject>Cloning, Molecular</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>CRYSTALS</subject><subject>DIFFUSION</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Hydro-Lyases - chemistry</subject><subject>Light</subject><subject>MAGNESIUM IONS</subject><subject>NHase</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Scattering, Radiation</subject><subject>Sepharose - chemistry</subject><subject>SPECIFICITY</subject><subject>STABILITY</subject><subject>X-RAY DIFFRACTION</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFks1u1DAUhSMEoqXwAGyQJSRWDfg6cRJvkMrQH1A1_BQErCyP4zQXHHuwPUB4EZ6Cl-DJyDCjUsSiC-tax9859pVvlt0F-hCA1o_OoC7LggqgnE6lENey3bWUr7Xrl_Y72a0YP1JaFKJqbmY7UHEABrCb_ZhZ79Cd75PlKmCHWiX0bp_oMMakrMXvfwSiXEuWwVgc0Kkwkvd5UCNpseuC0ltC2TFiJL4jDlNAa0g_tkElFQ3pgh9I6s16DX7Zo0VNniiN1q4iiQOmHpGczfJfP59TnsPt7EanbDR3tnUve3t0-GZ2kp--OH42OzjNNadQ57zgnIq6FZoxXjGhKi2gpVVXdJNaiaYpm1LTqgHVdmLB28pQXjaLBbTQ1cIUe9njTe5ytRhMq41LQVm5DDhMbUqvUP574rCX5_6LBFE3UJRTwP1NgI8JZdSYjO61d87oJBkreAUNm6gH22uC_7wyMckBozbWKmf8KsqaQsmYgCtBEA2rKBMTCBtQBx9jMN3Fm4HK9XTI_6Zj8ty73Oxfx3YcJkBsgK_T741XJ8qDD0fscM6B1ZM333gxJvPtwqvCJ1nVRc3lu_mxfCpentDX9Vy-Kn4D8FrXAw</recordid><startdate>200511</startdate><enddate>200511</enddate><creator>Hourai, Shinji</creator><creator>Ishii, Takeshi</creator><creator>Miki, Misao</creator><creator>Takashima, Yoshiki</creator><creator>Mitsuda, Satoshi</creator><creator>Yanagi, Kazunori</creator><general>Munksgaard International Publishers</general><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>200511</creationdate><title>Cloning, purification, crystallization and preliminary X-ray diffraction analysis of nitrile hydratase from the themophilic Bacillus smithii SC-J05-1</title><author>Hourai, Shinji ; Ishii, Takeshi ; Miki, Misao ; Takashima, Yoshiki ; Mitsuda, Satoshi ; Yanagi, Kazunori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5017-5355097d9c225629a6c91d06f3f97d6988484c0681adf9b5d6e0548bb1d1f79e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Bacillus - enzymology</topic><topic>Bacillus smithii</topic><topic>Chromatography</topic><topic>Cloning, Molecular</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>Crystallization Communications</topic><topic>Crystallography, X-Ray</topic><topic>CRYSTALS</topic><topic>DIFFUSION</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Hydro-Lyases - chemistry</topic><topic>Light</topic><topic>MAGNESIUM IONS</topic><topic>NHase</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Scattering, Radiation</topic><topic>Sepharose - chemistry</topic><topic>SPECIFICITY</topic><topic>STABILITY</topic><topic>X-RAY DIFFRACTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hourai, Shinji</creatorcontrib><creatorcontrib>Ishii, Takeshi</creatorcontrib><creatorcontrib>Miki, Misao</creatorcontrib><creatorcontrib>Takashima, Yoshiki</creatorcontrib><creatorcontrib>Mitsuda, Satoshi</creatorcontrib><creatorcontrib>Yanagi, Kazunori</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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F</addtitle><date>2005-11</date><risdate>2005</risdate><volume>61</volume><issue>11</issue><spage>974</spage><epage>977</epage><pages>974-977</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>Nitrile hydratase (NHase) converts nitriles to the corresponding amides and is recognized as having important industrial applications. Purification, cloning, crystallization and initial crystallographic studies of the NHase from Bacillus smithii SC‐J05‐1 (Bs NHase) were conducted to analyze the activity, specificity and thermal stability of this hydrolytic enzyme. Bs NHase was purified to homogeneity from microbial cells of B. smithii SC‐J05‐1 and the nucleotide sequences of both the α‐ and β‐subunits were determined. Purified Bs NHase was used for crystallization and several crystal forms were obtained by the vapour‐diffusion method. 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| ispartof | Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-11, Vol.61 (11), p.974-977 |
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| subjects | Bacillus - enzymology Bacillus smithii Chromatography Cloning, Molecular CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION Crystallization Communications Crystallography, X-Ray CRYSTALS DIFFUSION Electrophoresis, Polyacrylamide Gel Hydro-Lyases - chemistry Light MAGNESIUM IONS NHase Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Scattering, Radiation Sepharose - chemistry SPECIFICITY STABILITY X-RAY DIFFRACTION |
| title | Cloning, purification, crystallization and preliminary X-ray diffraction analysis of nitrile hydratase from the themophilic Bacillus smithii SC-J05-1 |
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