3DE1

Proteinase K by LB nanotemplate method after the third step of high X-Ray dose on ESRF ID23-1 beamline

Summary for 3DE1

Entry DOI	10.2210/pdb3de1/pdb
Related	3D9Q 3DDZ 3DE0 3DE2 3DE3 3DE4 3DE5 3DE6 3DE7
Descriptor	Proteinase K, CALCIUM ION (3 entities in total)
Functional Keywords	alpha beta protein, hydrolase, calcium, metal-binding, protease, serine protease, zymogen
Biological source	Engyodontium album (Engyodontium album)
Total number of polymer chains	1
Total formula weight	28970.86
Authors	Pechkova, E.,Tripathi, S.K.,Nicolini, C. (deposition date: 2008-06-07, release date: 2009-06-09, Last modification date: 2024-10-09)
Primary citation	Pechkova, E.,Tripathi, S.,Ravelli, R.B.,McSweeney, S.,Nicolini, C. Radiation stability of proteinase K crystals grown by LB nanotemplate method J.Struct.Biol., 168:409-418, 2009 Cited by PubMed Abstract: A detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method. PubMed: 19686853 DOI: 10.1016/j.jsb.2009.08.005 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation