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5EBH

Crystal Structure HEW Lysozyme processed with the CrystalDirect automated mounting and cryo-cooling technology

Summary for 5EBH
Entry DOI10.2210/pdb5ebh/pdb
DescriptorLysozyme C (2 entities in total)
Functional Keywordsglycosylase, hydrolase
Biological sourceGallus gallus (Chicken)
Cellular locationSecreted: P00698
Total number of polymer chains1
Total formula weight14331.16
Authors
Zander, U.,Hoffmann, G.,Cornaciu, I.,Marquez, J.A. (deposition date: 2015-10-19, release date: 2016-04-13, Last modification date: 2024-10-23)
Primary citationZander, U.,Hoffmann, G.,Cornaciu, I.,Marquette, J.P.,Papp, G.,Landret, C.,Seroul, G.,Sinoir, J.,Rower, M.,Felisaz, F.,Rodriguez-Puente, S.,Mariaule, V.,Murphy, P.,Mathieu, M.,Cipriani, F.,Marquez, J.A.
Automated harvesting and processing of protein crystals through laser photoablation.
Acta Crystallogr D Struct Biol, 72:454-466, 2016
Cited by
PubMed Abstract: Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.
PubMed: 27050125
DOI: 10.1107/S2059798316000954
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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