Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.
Recombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyeth...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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1995
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| _version_ | 1797097091142516736 |
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| author | Roach, P Schofield, C Baldwin, J Clifton, I Hajdu, J |
| author_facet | Roach, P Schofield, C Baldwin, J Clifton, I Hajdu, J |
| author_sort | Roach, P |
| collection | OXFORD |
| description | Recombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyethylene glycol 8000 as precipitant. The crystals (0.5-1.0 mm overall dimensions) diffract X-rays to at least 2.0 A resolution at synchrotrons and belong to space group P212121 with unit cell dimensions of a = 59.2 A, b = 127.0 A, and c = 139.6 A. The asymmetric unit contains one dimer, and the solvent content of the crystals is 60%. The crystals are radiation sensitive. |
| first_indexed | 2024-03-07T04:50:40Z |
| format | Journal article |
| id | oxford-uuid:d4d9c434-089c-4b2e-aa2f-421b8ccf12cb |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:50:40Z |
| publishDate | 1995 |
| record_format | dspace |
| spelling | oxford-uuid:d4d9c434-089c-4b2e-aa2f-421b8ccf12cb2022-03-27T08:21:37ZCrystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d4d9c434-089c-4b2e-aa2f-421b8ccf12cbEnglishSymplectic Elements at Oxford1995Roach, PSchofield, CBaldwin, JClifton, IHajdu, JRecombinant Aspergillus nidulans isopenicillin N synthase was purified from an Escherichia coli expression system. The apoenzyme in the presence of saturating concentrations of MnCl2 could be crystallized by either macro- or microseeding, using the hanging drop vapor diffusion technique with polyethylene glycol 8000 as precipitant. The crystals (0.5-1.0 mm overall dimensions) diffract X-rays to at least 2.0 A resolution at synchrotrons and belong to space group P212121 with unit cell dimensions of a = 59.2 A, b = 127.0 A, and c = 139.6 A. The asymmetric unit contains one dimer, and the solvent content of the crystals is 60%. The crystals are radiation sensitive. |
| spellingShingle | Roach, P Schofield, C Baldwin, J Clifton, I Hajdu, J Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title | Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title_full | Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title_fullStr | Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title_full_unstemmed | Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title_short | Crystallization and preliminary X-ray diffraction studies on recombinant isopenicillin N synthase from Aspergillus nidulans. |
| title_sort | crystallization and preliminary x ray diffraction studies on recombinant isopenicillin n synthase from aspergillus nidulans |
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