Introducing site‐specific cysteines into nanobodies for mercury labelling allows de novo phasing of their crystal structures

The generation of high‐quality protein crystals and the loss of phase information during an X‐ray crystallography diffraction experiment represent the major bottlenecks in the determination of novel protein structures. A generic method for introducing Hg atoms into any crystal independent of the pre...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2017-10, Vol.73 (10), p.804-813
Hauptverfasser:	Hansen, Simon Boje, Laursen, Nick Stub, Andersen, Gregers Rom, Andersen, Kasper R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies Atomic structure Camelids, New World Chemical compounds Complement C5 - immunology Complement component C5 Crystal structure Crystallization Crystallography Crystallography, X-Ray Crystals Cysteine Cysteine - chemistry Fluorescence Fluorophores Humans Labeling Mercury Mercury (metal) Mercury - chemistry Models, Molecular Nanobodies phasing Protein Conformation Protein structure Proteins Radiation effects Research Papers SAD single isomorphous replacement with anomalous signal Single-Domain Antibodies - chemistry Single-Domain Antibodies - immunology single‐wavelength anomalous dispersion SIRAS X-ray crystallography
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