1DWI

Study on radiation damage on a cryocooled crystal. Part 5: Structure after irradiation with 54.0*10e15 photons/mm2

1DWI の概要

• エントリーDOI: 10.2210/pdb1dwi/pdb
• 関連するPDBエントリー: 1DWA 1DWF 1DWG 1DWH 1DWJ 1MYR
• 分子名称: MYROSINASE MA1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-xylopyranose-(1-2)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: glycosidase, radiation damage, radiolysis, cryo-cooled, hydrolase
• 由来する生物種: SINAPIS ALBA (WHITE MUSTARD)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62372.43

構造登録者

Burmeister, W.P. (登録日: 1999-12-05, 公開日: 2000-03-03, 最終更新日: 2024-10-23)

主引用文献

Burmeister, W.P.
Structural Changes in a Cryo-Cooled Protein Crystal due to Radiation Damage
Acta Crystallogr.,Sect.D, 56:328-, 2000

PubMed Abstract: The high intensity of third-generation X-ray sources, along with the development of cryo-cooling of protein crystals at temperatures around 100 K, have made it possible to extend the diffraction limit of crystals and to reduce their size. However, even with cryo-cooled crystals, radiation damage becomes a limiting factor. So far, the radiation damage has manifested itself in the form of a loss of overall diffracted intensity and an increase in the temperature factor. The structure of a protein (myrosinase) after exposure to different doses of X-rays in the region of 20 x 10(15) photons mm(-2) has been studied. The changes in the structure owing to radiation damage were analysed using Fourier difference maps and occupancy refinement for the first time. Damage was obvious in the form of breakage of disulfide bonds, decarboxylation of aspartate and glutamate residues, a loss of hydroxyl groups from tyrosine and of the methylthio group of methionine. The susceptibility to radiation damage of individual groups of the same kind varies within the protein. The quality of the model resulting from structure determination might be compromised owing to the presence of radiolysis in the crystal after an excessive radiation dose. Radiation-induced structural changes may interfere with the interpretation of ligand-binding studies or MAD data. The experiments reported here suggest that there is an intrinsic limit to the amount of data which can be extracted from a sample of a given size.

PubMed: 10713520
DOI: 10.1107/S0907444999016261

実験手法

X-RAY DIFFRACTION (2 Å)