3DE7
Proteinase K by Classical hanging drop method after the fourth step of high X-Ray dose on ESRF ID23-1 beamline
Summary for 3DE7
Entry DOI | 10.2210/pdb3de7/pdb |
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: 2008-06-08, release date: 2009-06-09, Last modification date: 2024-11-06) |
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: 19686853DOI: 10.1016/j.jsb.2009.08.005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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