Structure determination by X-ray crystallography: analysis by X-rays and neutrons

2014 ◽  
Vol 20 (3) ◽  
pp. 235-236
Author(s):  
Tim Gruene
Keyword(s):  
Structure Determination ◽  
X Rays ◽  
X Ray ◽  
X Ray Crystallography

X-ray analysis

1999 ◽  
Author(s):  
L. Sawyer ◽  
M. A. Turner
Keyword(s):  
Structure Determination ◽  
Protein Crystallography ◽  
General Description ◽  
X Rays ◽  
Actual Structure ◽  
X Ray ◽  
Preliminary Characterization ◽  
X Ray Crystallography ◽  
Full Structure ◽  
Unit Cell Dimensions

This chapter covers the preliminary characterization of the crystals in order to determine if they are suitable for a full structure determination. Probably more frustrating than failure to produce crystals at all, is the growth of beautiful crystals which do not diffract, which have very large unit cell dimensions, or which decay very rapidly in the X-ray beam, though this last problem has been largely overcome by freezing the sample. It is impossible in one brief chapter to give more than a flavour of what the X-ray crystallographic technique entails and it is assumed that the protein chemist growing the crystals will have contact with a protein crystallographer, who will carry out the actual structure determination and in whose laboratory state-of-the-art facilities exist. However, preliminary characterization can often be carried out with little more than the equipment which is widely available in Chemistry and Physics Departments and so the crystal grower remote from a protein crystallography laboratory can monitor the success of their experiments. The reader should refer to the first edition for protocols useful for photographic characterization but such techniques are seldom used nowadays. It must be remembered, in any case, that X-rays are dangerous and the inexperienced should not try to X-ray protein crystals without help. It is necessary to provide an overview of X-ray crystallography, to put the preliminary characterization in context. For a general description of the technique the reader should refer to Glusker et al. (1) or Stout and Jensen (2). For protein crystallography in particular, the books by McRee (3) and Drenth (4) describe many of the advances since the seminal work of Blundell and Johnson (5). Amongst many excellent introductory articles, those by Bragg (6), published years ago, and Glusker (7) are particularly recommended. The scattering or diffraction of X-rays is an interference phenomenon and the interference between the X-rays scattered from the atoms in the structure produces significant changes in the observed diffraction in different directions. This variation in intensity with direction arises because the path differences taken by the scattered X-ray beams are of the same magnitude as the separation of the atoms in the molecule.

Frontier methods in coherent X-ray diffraction for high-resolution structure determination

2016 ◽  
Vol 49 ◽  
Author(s):  
Marcus Gallagher-Jones ◽  
Jose A. Rodriguez ◽  
Jianwei Miao
Keyword(s):  
Structure Determination ◽  
X Rays ◽  
X Ray Diffraction ◽  
Diffractive Imaging ◽  
X Ray ◽  
Coherent Diffractive Imaging ◽  
X Ray Crystallography ◽  
Max Von Laue ◽  
Complex Protein ◽  
High Resolution Structure

AbstractIn 1912, Max von Laue and collaborators first observed diffraction spots from a millimeter-sized crystal of copper sulfate using an X-ray tube. Crystallography was born of this experiment, and since then, diffraction by both X-rays and electrons has revealed a myriad of inorganic and organic structures, including structures of complex protein assemblies. Advancements in X-ray sources have spurred a revolution in structure determination, facilitated by the development of new methods. This review explores some of the frontier methods that are shaping the future of X-ray diffraction, including coherent diffractive imaging, serial femtosecond X-ray crystallography and small-angle X-ray scattering. Collectively, these methods expand the current limits of structure determination in biological systems across multiple length and time scales.

Beyond X-rays: an overview of emerging structural biology methods

2021 ◽  
Author(s):  
Jason E. Schaffer ◽  
Vandna Kukshal ◽  
Justin J. Miller ◽  
Vivian Kitainda ◽  
Joseph M. Jez
Keyword(s):  
Structure Determination ◽  
De Novo ◽  
Three Dimensional ◽  
Atomic Scale ◽  
X Rays ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Crystallography ◽  
New Methods ◽  
Main Technique

Structural biologists rely on X-ray crystallography as the main technique for determining the three-dimensional structures of macromolecules; however, in recent years, new methods that go beyond X-ray-based technologies are broadening the selection of tools to understand molecular structure and function. Simultaneously, national facilities are developing programming tools and maintaining personnel to aid novice structural biologists in de novo structure determination. The combination of X-ray free electron lasers (XFELs) and serial femtosecond crystallography (SFX) now enable time-resolved structure determination that allows for capture of dynamic processes, such as reaction mechanism and conformational flexibility. XFEL and SFX, along with microcrystal electron diffraction (MicroED), help side-step the need for large crystals for structural studies. Moreover, advances in cryogenic electron microscopy (cryo-EM) as a tool for structure determination is revolutionizing how difficult to crystallize macromolecules and/or complexes can be visualized at the atomic scale. This review aims to provide a broad overview of these new methods and to guide readers to more in-depth literature of these methods.

scholarly journals NSLS-II MX beamlines FMX for micro-crystallography & AMX for highly automated MX

2014 ◽  
Vol 70 (a1) ◽  
pp. C1733-C1733
Author(s):  
Martin Fuchs ◽  
Robert Sweet ◽  
Lonny Berman ◽  
Dileep Bhogadi ◽  
Wayne Hendrickson ◽  
...  
Keyword(s):  
Energy Range ◽  
Structure Determination ◽  
Optical Systems ◽  
Photon Flux ◽  
X Rays ◽  
Macromolecular Crystallography ◽  
Binding Studies ◽  
X Ray ◽  
Array Detectors ◽  
Broad Energy Range

We present the final design of the x-ray optical systems and experimental stations of the two macromolecular crystallography (MX) beamlines, FMX and AMX, at the National Synchrotron Light Source-II (NSLS-II). Along with its companion x-ray scattering beamline, LIX, this suite of Advanced Beamlines for Biological Investigations with X-rays (ABBIX, [1]) will begin user operation in 2016. The pair of MX beamlines with complementary and overlapping capabilities is located at canted undulators (IVU21) in sector 17-ID. The Frontier Microfocusing Macromolecular Crystallography beamline (FMX) will deliver a photon flux of ~5x10^12 ph/s at a wavelength of 1 Å into a spot of 1 - 50 µm size. It will cover a broad energy range from 5 - 30 keV, corresponding to wavelengths from 0.4 - 2.5 Å. The highly Automated Macromolecular Crystallography beamline (AMX) will be optimized for high throughput applications, with beam sizes from 4 - 100 µm, an energy range of 5 - 18 keV (0.7 - 2.5 Å), and a flux at 1 Å of ~10^13 ph/s. Central components of the in-house-developed experimental stations are a 100 nm sphere of confusion goniometer with a horizontal axis, piezo-slits to provide dynamic beam size changes during diffraction experiments, a dedicated secondary goniometer for crystallization plates, and sample- and plate-changing robots. FMX and AMX will support a broad range of biomedical structure determination methods from serial crystallography on micron-sized crystals, to structure determination of complexes in large unit cells, to rapid sample screening and data collection of crystals in trays, for instance to characterize membrane protein crystals and to conduct ligand-binding studies. Together with the solution scattering program at LIX, the new beamlines will offer unique opportunities for advanced diffraction experiments with micro- and mini-beams, with next generation hybrid pixel array detectors and emerging crystal delivery methods such as acoustic droplet ejection. This work is supported by the US National Institutes of Health.

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