1HJ8

1.00 AA Trypsin from Atlantic Salmon

1HJ8 の概要

• エントリーDOI: 10.2210/pdb1hj8/pdb
• 関連するPDBエントリー: 1BIT 1BZX 2STA 2STB
• 分子名称: TRYPSIN I, BENZAMIDINE, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, radiation damage, disulphide bond breakage, salmon, trypsin, atomic resolution
• 由来する生物種: SALMO SALAR (ATLANTIC SALMON)
• 細胞内の位置: Secreted, extracellular space: P35031
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24212.17

構造登録者

Leiros, H.-K.S.,Mcsweeney, S.M.,Smalas, A.O. (登録日: 2001-01-09, 公開日: 2002-01-04, 最終更新日: 2025-10-01)

主引用文献

Leiros, H.-K.S.,Mcsweeney, S.M.,Smalas, A.O.
Atomic Resolution Structure of Trypsin Provide Insight Into Structural Radiation Damage
Acta Crystallogr.,Sect.D, 57:488-, 2001

PubMed Abstract: Radiation damage is an inherent problem in protein X-ray crystallography and the process has recently been shown to be highly specific, exhibiting features such as cleavage of disulfide bonds, decarboxylation of acidic residues, increase in atomic B factors and increase in unit-cell volume. Reported here are two trypsin structures at atomic resolution (1.00 and 0.95 A), the data for which were collected at a third-generation synchrotron (ESRF) at two different beamlines. Both trypsin structures exhibit broken disulfide bonds; in particular, the bond from Cys191 to Cys220 is very sensitive to synchrotron radiation. The data set collected at the most intense beamline (ID14-EH4) shows increased structural radiation damage in terms of lower occupancies for cysteine residues, more breakage in the six disulfide bonds and more alternate conformations. It appears that high intensity and not only the total X-ray dose is most harmful to protein crystals.

PubMed: 11264577
DOI: 10.1107/S0907444901000646

実験手法

X-RAY DIFFRACTION (1 Å)