Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2
Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-diffusion method using 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl as precipitant. X-ray diffraction data were collected to 2.7 Å resolution using an in-house Bruker X8 PROTEUM single-crystal diffracto...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2010
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| Online Access: | http://psasir.upm.edu.my/id/eprint/13836/ http://psasir.upm.edu.my/id/eprint/13836/1/Crystallization%20and%20preliminary%20X.pdf |
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| author | Mohd Shariff, Fairolniza Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar |
| author_facet | Mohd Shariff, Fairolniza Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar |
| author_sort | Mohd Shariff, Fairolniza |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-diffusion method using 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl as precipitant. X-ray diffraction data were collected to 2.7 Å resolution using an in-house Bruker X8 PROTEUM single-crystal diffractometer system. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 87.44, b = 94.90, c = 126.46 Å. The asymmetric unit contained one single molecule of protein, with a Matthews coefficient (V M) of 2.85 Å3 Da−1 and a solvent content of 57%. |
| first_indexed | 2025-11-15T07:55:44Z |
| format | Article |
| id | upm-13836 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T07:55:44Z |
| publishDate | 2010 |
| publisher | International Union of Crystallography |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-138362016-09-28T02:41:03Z http://psasir.upm.edu.my/id/eprint/13836/ Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 Mohd Shariff, Fairolniza Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-diffusion method using 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl as precipitant. X-ray diffraction data were collected to 2.7 Å resolution using an in-house Bruker X8 PROTEUM single-crystal diffractometer system. The crystal belonged to the primitive orthorhombic space group P212121, with unit-cell parameters a = 87.44, b = 94.90, c = 126.46 Å. The asymmetric unit contained one single molecule of protein, with a Matthews coefficient (V M) of 2.85 Å3 Da−1 and a solvent content of 57%. International Union of Crystallography 2010-06-01 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/13836/1/Crystallization%20and%20preliminary%20X.pdf Mohd Shariff, Fairolniza and Raja Abdul Rahman, Raja Noor Zaliha and Mohamad Ali, Mohd Shukuri and Leow, Adam Thean Chor and Basri, Mahiran and Salleh, Abu Bakar (2010) Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66 (pt.6). pp. 715-717. ISSN 1744-3091 http://scripts.iucr.org/cgi-bin/paper?S174430911001482X 10.1107/S174430911001482X |
| spellingShingle | Mohd Shariff, Fairolniza Raja Abdul Rahman, Raja Noor Zaliha Mohamad Ali, Mohd Shukuri Leow, Adam Thean Chor Basri, Mahiran Salleh, Abu Bakar Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title | Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title_full | Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title_fullStr | Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title_full_unstemmed | Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title_short | Crystallization and preliminary X-ray crystallographic analysis of highly thermostable L2 lipase from the newly isolated Bacillus sp. L2 |
| title_sort | crystallization and preliminary x-ray crystallographic analysis of highly thermostable l2 lipase from the newly isolated bacillus sp. l2 |
| url | http://psasir.upm.edu.my/id/eprint/13836/ http://psasir.upm.edu.my/id/eprint/13836/ http://psasir.upm.edu.my/id/eprint/13836/ http://psasir.upm.edu.my/id/eprint/13836/1/Crystallization%20and%20preliminary%20X.pdf |