1HJ8

1.00 AA Trypsin from Atlantic Salmon

Summary for 1HJ8

• Entry DOI: 10.2210/pdb1hj8/pdb
• Related: 1BIT 1BZX 2STA 2STB
• Descriptor: TRYPSIN I, BENZAMIDINE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: hydrolase, radiation damage, disulphide bond breakage, salmon, trypsin, atomic resolution
• Biological source: SALMO SALAR (ATLANTIC SALMON)
• Cellular location: Secreted, extracellular space: P35031
• Total number of polymer chains: 1
• Total formula weight: 24212.17

Authors

Leiros, H.-K.S.,Mcsweeney, S.M.,Smalas, A.O. (deposition date: 2001-01-09, release date: 2002-01-04, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1 Å)