1XHO

Chorismate mutase from Clostridium thermocellum Cth-682

1XHO の概要

• エントリーDOI: 10.2210/pdb1xho/pdb
• 分子名称: Chorismate mutase, UNKNOWN ATOM OR ION (3 entities in total)
• 機能のキーワード: chorismate mutase, clostridium thermocellum, southeast collaboratory for structural genomics, secsg, protein structure initiative, psi, structural genomics, unknown function
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 50099.75

構造登録者

Xu, H.,Chen, L.,Lee, D.,Habel, J.E.,Nguyen, J.,Chang, S.-H.,Kataeva, I.,Chang, J.,Zhao, M.,Yang, H.,Horanyi, P.,Florence, Q.,Tempel, W.,Zhou, W.,Lin, D.,Zhang, H.,Praissman, J.,Arendall III, W.B.,Richardson, J.S.,Richardson, D.C.,Ljungdahl, L.,Liu, Z.-J.,Rose, J.P.,Wang, B.-C.,Southeast Collaboratory for Structural Genomics (SECSG) (登録日: 2004-09-20, 公開日: 2004-11-23, 最終更新日: 2024-11-13)

主引用文献

Xu, H.,Yang, C.,Chen, L.,Kataeva, I.A.,Tempel, W.,Lee, D.,Habel, J.E.,Nguyen, D.,Pflugrath, J.W.,Ferrara, J.D.,Arendall, W.B.,Richardson, J.S.,Richardson, D.C.,Liu, Z.J.,Newton, M.G.,Rose, J.P.,Wang, B.C.
Away from the edge II: in-house Se-SAS phasing with chromium radiation.
Acta Crystallogr.,Sect.D, 61:960-966, 2005

PubMed Abstract: 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.

PubMed: 15983419
DOI: 10.1107/S0907444905010644

実験手法

X-RAY DIFFRACTION (2.2 Å)