7L84

Hen Egg White Lysozyme by Native S-SAD at Room Temperature

Summary for 7L84

• Entry DOI: 10.2210/pdb7l84/pdb
• Descriptor: Lysozyme C (2 entities in total)
• Functional Keywords: hydrolase, lysozyme
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Greisman, J.B.,Dalton, K.M.,Hekstra, D.R. (deposition date: 2020-12-30, release date: 2021-01-13, Last modification date: 2024-10-16)

Primary citation

Greisman, J.B.,Dalton, K.M.,Sheehan, C.J.,Klureza, M.A.,Kurinov, I.,Hekstra, D.R.
Native SAD phasing at room temperature.
Acta Crystallogr D Struct Biol, 78:986-996, 2022

PubMed Abstract: Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature.

PubMed: 35916223
DOI: 10.1107/S2059798322006799

Experimental method

X-RAY DIFFRACTION (1.7 Å)