1hj8
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1.00 AA TRYPSIN FROM ATLANTIC SALMON
OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
1HJ8 is a [Single protein] structure of sequence from [Salmo salar] with SO4, CA and BAM as [ligands]. Active as [[1]], with EC number [3.4.21.4]. Full crystallographic information is available from [OCA].
ReferenceReference
Atomic resolution structures of trypsin provide insight into structural radiation damage., Leiros HK, McSweeney SM, Smalas AO, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):488-97. PMID:11264577
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