Crystal structure of chicken egg lysozyme at ambient temperatureCrystal structure of chicken egg lysozyme at ambient temperature

Structural highlights

8h3w is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.39Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]

Publication Abstract from PubMed

High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Serial crystallography is an emerging structural biology technique which has fundamental limitations due to either sample volume requirements or immediate access to the competitive X-ray beamtime. Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography. As an alternative, we introduce the plate-reader module adapted for using a 72-well Terasaki plate for biomacromolecule structure determination at a convenience of a home X-ray source. We also present the first ambient temperature lysozyme structure determined at the Turkish light source (Turkish DeLight). The complete dataset was collected in 18.5 min with resolution extending to 2.39 A and 100% completeness. Combined with our previous cryogenic structure (PDB ID: 7Y6A), the ambient temperature structure provides invaluable information about the structural dynamics of the lysozyme. Turkish DeLight provides robust and rapid ambient temperature biomacromolecular structure determination with limited radiation damage.

Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source.,Gul M, Ayan E, Destan E, Johnson JA, Shafiei A, Kepceoglu A, Yilmaz M, Ertem FB, Yapici I, Tosun B, Baldir N, Tokay N, Nergiz Z, Karakadioglu G, Paydos SS, Kulakman C, Ferah CK, Guven O, Atalay N, Akcan EK, Cetinok H, Arslan NE, Sabanoglu K, Asci B, Tavli S, Gumusboga H, Altuntas S, Otsuka M, Fujita M, Teki N S, Ci Ftci H, Durdagi S, Karaca E, Kaplan Turkoz B, Kabasakal BV, Kati A, DeMi Rci H Sci Rep. 2023 May 19;13(1):8123. doi: 10.1038/s41598-023-33989-0. PMID:37208392[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Gul M, Ayan E, Destan E, Johnson JA, Shafiei A, Kepceoğlu A, Yilmaz M, Ertem FB, Yapici İ, Tosun B, Baldir N, Tokay N, Nergiz Z, Karakadioğlu G, Paydos SS, Kulakman C, Ferah CK, Güven Ö, Atalay N, Akcan EK, Cetinok H, Arslan NE, Şabanoğlu K, Aşci B, Tavli S, Gümüsboğa H, Altuntaş S, Otsuka M, Fujita M, Teki N Ş, Çi Ftçi H, Durdaği S, Karaca E, Kaplan Türköz B, Kabasakal BV, Kati A, DeMi Rci H. Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source. Sci Rep. 2023 May 19;13(1):8123. PMID:37208392 doi:10.1038/s41598-023-33989-0

8h3w, resolution 2.39Å

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