Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus
The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P2{sub 1} and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively. The Gram-negative aerobic eubacterium Thermus thermophilus is an extremely important thermop...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2007-01, Vol.63 (Pt 1) |
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| creator | Kanaujia, Shankar Prasad Ranjani, Chellamuthu Vasuki Jeyakanthan, Jeyaraman Baba, Seiki Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 Chen, Lirong Liu, Zhi-Jie Wang, Bi-Cheng Nishida, Masami Ebihara, Akio Shinkai, Akeo Kuramitsu, Seiki Shiro, Yoshitsugu Sekar, Kanagaraj Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012 Yokoyama, Shigeyuki RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045 Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033 Bioinformatics Centre |
| description | The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P2{sub 1} and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively. The Gram-negative aerobic eubacterium Thermus thermophilus is an extremely important thermophilic microorganism that was originally isolated from a thermal vent environment in Japan. The molybdenum cofactor in this organism is considered to be an essential component required by enzymes that catalyze diverse key reactions in the global metabolism of carbon, nitrogen and sulfur. The molybdenum-cofactor biosynthesis protein C derived from T. thermophilus was crystallized in two different space groups. Crystals obtained using the first crystallization condition belong to the monoclinic space group P2{sub 1}, with unit-cell parameters a = 64.81, b = 109.84, c = 115.19 Å, β = 104.9°; the crystal diffracted to a resolution of 1.9 Å. The other crystal form belonged to space group R32, with unit-cell parameters a = b = 106.57, c = 59.25 Å, and diffracted to 1.75 Å resolution. Preliminary calculations reveal that the asymmetric unit contains 12 monomers and one monomer for the crystals belonging to space group P2{sub 1} and R32, respectively. |
| doi_str_mv | 10.1107/S1744309106052560 |
| format | Article |
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The Gram-negative aerobic eubacterium Thermus thermophilus is an extremely important thermophilic microorganism that was originally isolated from a thermal vent environment in Japan. The molybdenum cofactor in this organism is considered to be an essential component required by enzymes that catalyze diverse key reactions in the global metabolism of carbon, nitrogen and sulfur. The molybdenum-cofactor biosynthesis protein C derived from T. thermophilus was crystallized in two different space groups. Crystals obtained using the first crystallization condition belong to the monoclinic space group P2{sub 1}, with unit-cell parameters a = 64.81, b = 109.84, c = 115.19 Å, β = 104.9°; the crystal diffracted to a resolution of 1.9 Å. The other crystal form belonged to space group R32, with unit-cell parameters a = b = 106.57, c = 59.25 Å, and diffracted to 1.75 Å resolution. Preliminary calculations reveal that the asymmetric unit contains 12 monomers and one monomer for the crystals belonging to space group P2{sub 1} and R32, respectively.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S1744309106052560</identifier><language>eng</language><publisher>United Kingdom</publisher><subject>CARBON ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; CRYSTALLIZATION ; CRYSTALS ; ENVIRONMENT ; IRON ; MOLYBDENUM ; MONOMERS ; NITROGEN ; RESOLUTION ; SPACE GROUPS ; SULFUR</subject><ispartof>Acta crystallographica. 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Section F, Structural biology and crystallization communications</title><description>The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P2{sub 1} and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively. The Gram-negative aerobic eubacterium Thermus thermophilus is an extremely important thermophilic microorganism that was originally isolated from a thermal vent environment in Japan. The molybdenum cofactor in this organism is considered to be an essential component required by enzymes that catalyze diverse key reactions in the global metabolism of carbon, nitrogen and sulfur. The molybdenum-cofactor biosynthesis protein C derived from T. thermophilus was crystallized in two different space groups. Crystals obtained using the first crystallization condition belong to the monoclinic space group P2{sub 1}, with unit-cell parameters a = 64.81, b = 109.84, c = 115.19 Å, β = 104.9°; the crystal diffracted to a resolution of 1.9 Å. The other crystal form belonged to space group R32, with unit-cell parameters a = b = 106.57, c = 59.25 Å, and diffracted to 1.75 Å resolution. Preliminary calculations reveal that the asymmetric unit contains 12 monomers and one monomer for the crystals belonging to space group P2{sub 1} and R32, respectively.</description><subject>CARBON</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>CRYSTALS</subject><subject>ENVIRONMENT</subject><subject>IRON</subject><subject>MOLYBDENUM</subject><subject>MONOMERS</subject><subject>NITROGEN</subject><subject>RESOLUTION</subject><subject>SPACE GROUPS</subject><subject>SULFUR</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqNjD1PwzAURS0EEuXjB7A9iTlgx0lK5wjETvfKdZ3mVbZf5OcMZuOf00gdGJnu1blHV4gnJV-UkuvXL7VuGi03SnayrdtOXonVgqqFXf_pt-KO-SSl1pvubSV--lQ4G-_x22SkCCYeYErOY8BoUgF72emYzDSiPQvGF0YGGiCQL_uDi3OoLA3GZkqwR-IS8-gWZ0qUHUboYUgUYDu6FGaGvCSd7_zMD-JmMJ7d4yXvxfPH-7b_rIgz7thidna0FKOzeVfXupN10-r_Wb8Nj1qc</recordid><startdate>20070101</startdate><enddate>20070101</enddate><creator>Kanaujia, Shankar Prasad</creator><creator>Ranjani, Chellamuthu Vasuki</creator><creator>Jeyakanthan, Jeyaraman</creator><creator>Baba, Seiki</creator><creator>Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043</creator><creator>Chen, Lirong</creator><creator>Liu, Zhi-Jie</creator><creator>Wang, Bi-Cheng</creator><creator>Nishida, Masami</creator><creator>Ebihara, Akio</creator><creator>Shinkai, Akeo</creator><creator>Kuramitsu, Seiki</creator><creator>Shiro, Yoshitsugu</creator><creator>Sekar, Kanagaraj</creator><creator>Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012</creator><creator>Yokoyama, Shigeyuki</creator><creator>RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045</creator><creator>Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</creator><creator>Bioinformatics Centre</creator><scope>OTOTI</scope></search><sort><creationdate>20070101</creationdate><title>Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus</title><author>Kanaujia, Shankar Prasad ; Ranjani, Chellamuthu Vasuki ; Jeyakanthan, Jeyaraman ; Baba, Seiki ; Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 ; Chen, Lirong ; Liu, Zhi-Jie ; Wang, Bi-Cheng ; Nishida, Masami ; Ebihara, Akio ; Shinkai, Akeo ; Kuramitsu, Seiki ; Shiro, Yoshitsugu ; Sekar, Kanagaraj ; Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012 ; Yokoyama, Shigeyuki ; RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045 ; Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033 ; Bioinformatics Centre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-osti_scitechconnect_223602453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>CARBON</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>CRYSTALS</topic><topic>ENVIRONMENT</topic><topic>IRON</topic><topic>MOLYBDENUM</topic><topic>MONOMERS</topic><topic>NITROGEN</topic><topic>RESOLUTION</topic><topic>SPACE GROUPS</topic><topic>SULFUR</topic><toplevel>online_resources</toplevel><creatorcontrib>Kanaujia, Shankar Prasad</creatorcontrib><creatorcontrib>Ranjani, Chellamuthu Vasuki</creatorcontrib><creatorcontrib>Jeyakanthan, Jeyaraman</creatorcontrib><creatorcontrib>Baba, Seiki</creatorcontrib><creatorcontrib>Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043</creatorcontrib><creatorcontrib>Chen, Lirong</creatorcontrib><creatorcontrib>Liu, Zhi-Jie</creatorcontrib><creatorcontrib>Wang, Bi-Cheng</creatorcontrib><creatorcontrib>Nishida, Masami</creatorcontrib><creatorcontrib>Ebihara, Akio</creatorcontrib><creatorcontrib>Shinkai, Akeo</creatorcontrib><creatorcontrib>Kuramitsu, Seiki</creatorcontrib><creatorcontrib>Shiro, Yoshitsugu</creatorcontrib><creatorcontrib>Sekar, Kanagaraj</creatorcontrib><creatorcontrib>Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><creatorcontrib>RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045</creatorcontrib><creatorcontrib>Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</creatorcontrib><creatorcontrib>Bioinformatics Centre</creatorcontrib><collection>OSTI.GOV</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanaujia, Shankar Prasad</au><au>Ranjani, Chellamuthu Vasuki</au><au>Jeyakanthan, Jeyaraman</au><au>Baba, Seiki</au><au>Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043</au><au>Chen, Lirong</au><au>Liu, Zhi-Jie</au><au>Wang, Bi-Cheng</au><au>Nishida, Masami</au><au>Ebihara, Akio</au><au>Shinkai, Akeo</au><au>Kuramitsu, Seiki</au><au>Shiro, Yoshitsugu</au><au>Sekar, Kanagaraj</au><au>Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012</au><au>Yokoyama, Shigeyuki</au><au>RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045</au><au>Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033</au><au>Bioinformatics Centre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><date>2007-01-01</date><risdate>2007</risdate><volume>63</volume><issue>Pt 1</issue><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>The molybdenum-cofactor biosynthesis protein C from T. thermophilus has been crystallized in two different space groups, P2{sub 1} and R32; the crystals diffracted to 1.9 and 1.75 Å resolution, respectively. The Gram-negative aerobic eubacterium Thermus thermophilus is an extremely important thermophilic microorganism that was originally isolated from a thermal vent environment in Japan. The molybdenum cofactor in this organism is considered to be an essential component required by enzymes that catalyze diverse key reactions in the global metabolism of carbon, nitrogen and sulfur. The molybdenum-cofactor biosynthesis protein C derived from T. thermophilus was crystallized in two different space groups. Crystals obtained using the first crystallization condition belong to the monoclinic space group P2{sub 1}, with unit-cell parameters a = 64.81, b = 109.84, c = 115.19 Å, β = 104.9°; the crystal diffracted to a resolution of 1.9 Å. The other crystal form belonged to space group R32, with unit-cell parameters a = b = 106.57, c = 59.25 Å, and diffracted to 1.75 Å resolution. Preliminary calculations reveal that the asymmetric unit contains 12 monomers and one monomer for the crystals belonging to space group P2{sub 1} and R32, respectively.</abstract><cop>United Kingdom</cop><doi>10.1107/S1744309106052560</doi></addata></record> |
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| subjects | CARBON CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION CRYSTALS ENVIRONMENT IRON MOLYBDENUM MONOMERS NITROGEN RESOLUTION SPACE GROUPS SULFUR |
| title | Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus |
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