4ZG3 image
Deposition Date 2015-04-22
Release Date 2016-03-09
Last Version Date 2024-11-13
Entry Detail
PDB ID:
4ZG3
Keywords:
Title:
In-vacuum long-wavelength crystallography
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
1.20 Å
R-Value Free:
0.16
R-Value Work:
0.14
R-Value Observed:
0.14
Space Group:
P 41 21 2
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:Thaumatin-1
Chain IDs:A
Chain Length:207
Number of Molecules:1
Biological Source:Thaumatococcus daniellii
Primary Citation
In-vacuum long-wavelength macromolecular crystallography.
Acta Crystallogr D Struct Biol 72 430 439 (2016)
PMID: 26960130 DOI: 10.1107/S2059798316001078

Abstact

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.

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Primary Citation of related structures
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