6APM

Hen egg-white lysozyme (WT), solved with serial millisecond crystallography using synchrotron radiation

Summary for 6APM

• Entry DOI: 10.2210/pdb6apm/pdb
• Related: 6APF 6APG 6APK
• Descriptor: Lysozyme C, SODIUM ION (3 entities in total)
• Functional Keywords: hewl, lysozyme, xfel crystal structure, serial millisecond crystallography, hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14354.15

Authors

Lyubimov, A.Y.,Mathews, I.I.,Uervivojnangkoorn, M.,Soltis, S.M.,Cohen, A.E. (deposition date: 2017-08-17, release date: 2018-04-04, Last modification date: 2024-10-09)

Primary citation

Mathews, I.I.,Allison, K.,Robbins, T.,Lyubimov, A.Y.,Uervirojnangkoorn, M.,Brunger, A.T.,Khosla, C.,DeMirci, H.,McPhillips, S.E.,Hollenbeck, M.,Soltis, M.,Cohen, A.E.
The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography.
Biochemistry, 56:4751-4756, 2017

PubMed Abstract: The crystal structure of the trans-acyltransferase (AT) from the disorazole polyketide synthase (PKS) was determined at room temperature to a resolution of 2.5 Å using a new method for the direct delivery of the sample into an X-ray free-electron laser. A novel sample extractor efficiently delivered limited quantities of microcrystals directly from the native crystallization solution into the X-ray beam at room temperature. The AT structure revealed important catalytic features of this core PKS enzyme, including the occurrence of conformational changes around the active site. The implications of these conformational changes for polyketide synthase reaction dynamics are discussed.

PubMed: 28832129
DOI: 10.1021/acs.biochem.7b00711

Experimental method

X-RAY DIFFRACTION (2.05 Å)