2E6U

Crystal structure of hypothetical protein PH1109 from Pyrococcus horikoshii

「2CZZ」から置き換えられました

2E6U の概要

• エントリーDOI: 10.2210/pdb2e6u/pdb
• 分子名称: hypothetical protein PH1109, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: rossmann-like, coa binding, structural genomics consortium for research on gene expression system, structural genomics, unknown function
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17661.40

構造登録者

Kitago, Y.,Min, Y.,Watanabe, N.,Tanaka, I. (登録日: 2007-01-03, 公開日: 2007-01-23, 最終更新日: 2024-03-13)

主引用文献

Kitago, Y.,Watanabe, N.,Tanaka, I.
Structure determination of a novel protein by sulfur SAD using chromium radiation in combination with a new crystal-mounting method
ACTA CRYSTALLOGR.,SECT.D, 61:1013-1021, 2005

PubMed Abstract: A novel and easy crystal-mounting technique was developed for the sulfur SAD method using Cr Kalpha radiation (2.29 A). Using this technique, the cryo-buffer and cryoloop around the protein crystal can be removed before data collection in order to eliminate their X-ray absorption. The superiority and reproducibility of the data sets with this mounting technique were demonstrated using tetragonal hen egg-white lysozyme crystals. The structure of a novel protein, PH1109, from Pyrococcus horikoshii OT3 was solved using this technique. At the wavelength of Cr Kalpha radiation, the anomalous signal |DeltaF|/|F| of PH1109 is expected to be 1.72% as this protein of 144 residues includes four methionines and two cysteines. Sulfur SAD phasing was performed using SHELXD and SHELXE. In the case of the data set obtained using this novel crystal-mounting technique, 54.9% of all residues were built with side chains automatically by RESOLVE. On the other hand, only 16.0% were built with side chains for the data set collected using the standard cryoloop. These results indicated that this crystal-mounting technique was superior to the standard loop-mounting method for the measurement of small anomalous differences at longer wavelength and yielded better results in sulfur-substructure solution and initial phasing. The present study demonstrates that the sulfur SAD method with a chromium source becomes enhanced and more practical for macromolecular structure determination using the new crystal-mounting technique.

PubMed: 16041065
DOI: 10.1107/S0907444905012734

実験手法

X-RAY DIFFRACTION (1.8 Å)