4ZG3

In-vacuum long-wavelength crystallography

Summary for 4ZG3

• Entry DOI: 10.2210/pdb4zg3/pdb
• Descriptor: Thaumatin-1, L(+)-TARTARIC ACID, GLYCEROL, ... (5 entities in total)
• Functional Keywords: thaumatin, in vacuum, plant protein
• Biological source: Thaumatococcus daniellii (Katemfe)
• Cellular location: Cytoplasmic vesicle: P02883
• Total number of polymer chains: 1
• Total formula weight: 22849.36

Authors

Wagner, A.,Duman, R.,Henderson, K.,Mykhaylyk, V. (deposition date: 2015-04-22, release date: 2016-03-09, Last modification date: 2024-11-13)

Primary citation

Wagner, A.,Duman, R.,Henderson, K.,Mykhaylyk, V.
In-vacuum long-wavelength macromolecular crystallography.
Acta Crystallogr D Struct Biol, 72:430-439, 2016

PubMed Abstract: Structure solution based on the weak anomalous signal from native (protein and DNA) crystals is increasingly being attempted as part of synchrotron experiments. Maximizing the measurable anomalous signal by collecting diffraction data at longer wavelengths presents a series of technical challenges caused by the increased absorption of X-rays and larger diffraction angles. A new beamline at Diamond Light Source has been built specifically for collecting data at wavelengths beyond the capability of other synchrotron macromolecular crystallography beamlines. Here, the theoretical considerations in support of the long-wavelength beamline are outlined and the in-vacuum design of the endstation is discussed, as well as other hardware features aimed at enhancing the accuracy of the diffraction data. The first commissioning results, representing the first in-vacuum protein structure solution, demonstrate the promising potential of the beamline.

PubMed: 26960130
DOI: 10.1107/S2059798316001078

Experimental method

X-RAY DIFFRACTION (1.2 Å)