1xho
From Proteopedia
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'''Chorismate mutase from Clostridium thermocellum Cth-682''' | '''Chorismate mutase from Clostridium thermocellum Cth-682''' | ||
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[[Category: Zhao, M.]] | [[Category: Zhao, M.]] | ||
[[Category: Zhou, W.]] | [[Category: Zhou, W.]] | ||
| - | [[Category: | + | [[Category: Chorismate mutase]] |
| - | [[Category: | + | [[Category: Clostridium thermocellum]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Secsg]] |
| - | [[Category: | + | [[Category: Southeast collaboratory for structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:02:47 2008'' | |
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Revision as of 12:02, 3 May 2008
Chorismate mutase from Clostridium thermocellum Cth-682
Overview
Recently, the demands of high-throughput macromolecular crystallography have driven continuous improvements in phasing methods, data-collection protocols and many other technologies. Single-wavelength anomalous scattering (SAS) phasing with chromium X-ray radiation opens a new possibility for phasing a protein with data collected in-house and has led to several successful examples of de novo structure solution using only weak anomalous scatterers such as sulfur. To further reduce data-collection time and make SAS phasing more robust, it is natural to combine selenomethionine-derivatized protein (SeMet protein) with Cr Kalpha radiation to take advantage of the larger anomalous scattering signal from selenium (f = 2.28 e(-)) compared with sulfur (f = 1.14 e(-)). As reported herein, the crystal structure of a putative chorismate mutase from Clostridium thermocellum was determined using Se-SAS with Cr Kalpha radiation. Each protein molecule contains eight selenomethionine residues in 148 amino-acid residues, providing a calculated Bijvoet ratio of about 3.5% at the Cr Kalpha wavelength. A single data set to 2.2 A resolution with approximately ninefold redundancy was collected using an imaging-plate detector coupled with a Cr source. Structure solution, refinement and deposition to the Protein Data Bank were performed within 9 h of the availability of the scaled diffraction data. The procedure used here is applicable to many other proteins and promises to become a routine pathway for in-house high-throughput crystallography.
About this Structure
1XHO is a Single protein structure of sequence from Clostridium thermocellum. Full crystallographic information is available from OCA.
Reference
Away from the edge II: in-house Se-SAS phasing with chromium radiation., Xu H, Yang C, Chen L, Kataeva IA, Tempel W, Lee D, Habel JE, Nguyen D, Pflugrath JW, Ferrara JD, Arendall WB 3rd, Richardson JS, Richardson DC, Liu ZJ, Newton MG, Rose JP, Wang BC, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):960-6. Epub 2005, Jun 24. PMID:15983419 Page seeded by OCA on Sat May 3 15:02:47 2008
Categories: Clostridium thermocellum | Single protein | Chang, J. | Chang, S H. | Chen, L. | Florence, Q. | Habel, J E. | Horanyi, P. | III, W B.Arendall. | Kataeva, I. | Lee, D. | Lin, D. | Liu, Z J. | Ljungdahl, L. | Nguyen, J. | Praissman, J. | Richardson, D C. | Richardson, J S. | Rose, J P. | SECSG, Southeast Collaboratory for Structural Genomics. | Tempel, W. | Wang, B C. | Xu, H. | Yang, H. | Zhang, H. | Zhao, M. | Zhou, W. | Chorismate mutase | Protein structure initiative | Psi | Secsg | Southeast collaboratory for structural genomic
