Crystallization and preliminary X-ray diffraction analysis of Hypocrea jecorina Cel7A in two new crystal forms
| Autor: | Annette M. Bodenheimer, Paul Swartz, Barbara R. Evans, Junhong He, Dean A. A. Myles, Matthew J. Cuneo, Flora Meilleur, Hugh O'Neill |
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| Rok vydání: | 2014 |
| Předmět: |
Diffraction
Materials science biology Hypocrea Resolution (electron density) Biophysics Condensed Matter Physics biology.organism_classification Crystallography X-Ray Biochemistry law.invention Preliminary analysis Crystal Crystallography Structural Biology law Crystallization Communications X-ray crystallography Genetics Cellulose 1 4-beta-Cellobiosidase Electrophoresis Polyacrylamide Gel Crystallization Linker |
| Zdroj: | Acta crystallographica. Section F, Structural biology communications. 70(Pt 6) |
| ISSN: | 2053-230X |
| Popis: | Cel7A (previously known as cellobiohydrolase I) fromHypocrea jecorinawas crystallized in two crystalline forms, neither of which have been previously reported. Both forms co-crystallize under the same crystallization conditions. The first crystal form belonged to space groupC2, with unit-cell parametersa= 152.5,b= 44.9,c= 57.6 Å, β = 101.2°, and diffracted X-rays to 1.5 Å resolution. The second crystal form belonged to space groupP6322, with unit-cell parametersa=b≃ 155,c≃ 138 Å, and diffracted X-rays to 2.5 Å resolution. The crystals were obtained using full-length Cel7A, which consists of a large 434-residue N-terminal catalytic domain capable of cleaving cellulose, a 27-residue flexible linker and a small 36-residue C-terminal carbohydrate-binding module (CBM). However, a preliminary analysis of the electron-density maps suggests that the linker and CBM are disordered in both crystal forms. Complete refinement and structure analysis are currently in progress. |
| Databáze: | OpenAIRE |
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