5KKJ

2.0-Angstrom In situ Mylar structure of hen egg-white lysozyme (HEWL) at 293 K

Summary for 5KKJ

• Entry DOI: 10.2210/pdb5kkj/pdb
• Related: 5KKH 5KKI 5KKK
• Descriptor: Lysozyme C, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: hydrolase
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14883.60

Authors

Broecker, J.,Ernst, O.P. (deposition date: 2016-06-21, release date: 2017-02-15, Last modification date: 2024-10-23)

Primary citation

Broecker, J.,Klingel, V.,Ou, W.L.,Balo, A.R.,Kissick, D.J.,Ogata, C.M.,Kuo, A.,Ernst, O.P.
A Versatile System for High-Throughput In Situ X-ray Screening and Data Collection of Soluble and Membrane-Protein Crystals.
Cryst Growth Des, 16:6318-6326, 2016

PubMed Abstract: In recent years, in situ data collection has been a major focus of progress in protein crystallography. Here, we introduce the Mylar in situ method using Mylar-based sandwich plates that are inexpensive, easy to make and handle, and show significantly less background scattering than other setups. A variety of cognate holders for patches of Mylar in situ sandwich films corresponding to one or more wells makes the method robust and versatile, allows for storage and shipping of entire wells, and enables automated crystal imaging, screening, and goniometer-based X-ray diffraction data-collection at room temperature and under cryogenic conditions for soluble and membrane-protein crystals grown in or transferred to these plates. We validated the Mylar in situ method using crystals of the water-soluble proteins hen egg-white lysozyme and sperm whale myoglobin as well as the 7-transmembrane protein bacteriorhodopsin from . In conjunction with current developments at synchrotrons, this approach promises high-resolution structural studies of membrane proteins to become faster and more routine.

PubMed: 28261000
DOI: 10.1021/acs.cgd.6b00950

Experimental method

X-RAY DIFFRACTION (2.001 Å)