Protein Micro-Crystallography: Nanotechnology Challenges Ahead

Christian Riekel

ESRF-The European Synchrotron, CS40220, F-38043 Grenoble Cedex 9, France


The status and prospects of protein microcrystallography (MPX) at high brilliance synchrotron radiation sources are reviewed. We discuss emerging trends in miniaturizing sample environments for serial crystallography (SX) experiments allowing manipulation and positioning of biological objects down to nanoscale dimensions with low contact forces.


Synchrotron radiation, X-ray free electron laser, Protein microcrystallography, Serial crystallography, Nanotechnology, Sample environment


MPX: Protein Microcrystallography; SR: Synchrotron Radiation; SX: Serial Crystallography; SFX: Serial Femtosecond Crystallography; SSX: Synchrotron Serial Crystallography; XFEL: X-ray Free Electron Laser; TMV: Tobacco Mosaic Virus


Protein microcrystallography (MPX) at 3rd generation synchrotron radiation (SR) sources [1, 2] has provided access to structures which are difficult to crystallize such as amyloids [3] or membrane proteins [4, 5]. Technical and scientific progress is dominated by the development of more and more brilliant X-ray sources allowing recording diffraction patterns from increasingly smaller crystals in a shorter time. X-ray free electron laser sources (XFEL), such as the Linac Coherent Light Source (LCLS, Stanford, California, USA) have profoundly modified MPX [6, 7]. Indeed, femtosecond X-ray flashes from XFELs allow obtaining quasi radiation-damage-free diffraction data from nm-sized crystallites in a hitand- destroy mode [7-9]. This has resulted in serial femtosecond crystallography (SFX) techniques based on the merging of patterns due to hits from thousands of crystallites [10]. Indeed, a microjet injector containing photosystem I crystallites down to 200 nm size was used for the first SFX experiment (Figure 1) [9, 11]. For an overview on other SFX flow-injectors and fixed target supports see: [12].The limited availability of XFELs provides, however, a drive for optimizing SR-MPX beam lines and using both types of sources in a complementary way. Indeed, SR-MPX provides currently access to crystallite volumes down to a few μm3 [1, 2, 13] while nm3 volumes have become accessible at XFELs [9]. Radiation-free XFEL data collection is a dream-come-true for protein crystallographers. SRexperiments provide, however, more flexibility for in-situ sample environments such as crystallization plates or microfluidic devices. Special care has, however, to be taken to minimize radiation damage in SR-MPX experiments.

In the following we will first review several emerging trends for SR-MPX with beam sizes from the μm- to the nmrange and then highlight the potential of advanced sample environments. Rather than being exhaustive we will focus on selected on-chip sample environments and low contact-force manipulation derived from nanobiotechnology tools and techniques [14]. The term “MPX” will be used independently of the X-ray beam size.

Sources and Beamlines

A comparison of the brilliance (corresponding to the photon concentration; also called spectral brightness) of 3rd generation SR sources shows the progress in maximum brilliance for the most recent SR sources (e.g. MAX IV, [15] NSLS II [16]) which are based on advanced magnet lattice designs (Figure 2A). The correlation of focal spot size and maximum flux density of a number of SR-MPX beam lines worldwide reveals that the most advanced SR sources aim for a particularly high (monochromatic) flux density of ~1013 photons/(s, μm2) for an ~1 μm2 focus (Figure 2B); (FMXNSLS II beamline). The drive towards higher SR brilliances is, however, continuing. Indeed, the brilliance depends on the horizontal and vertical emittance (εhor,vert) of the electron beam in a storage ring which is the product of its size (δhor,vert) and divergence (δ'hor,vert). The emittance can be reduced by a compression of the electron beam up to its theoretical limit when electron diffraction effects set in. This limit defines a 4th generation (“diffraction limited”) SR source [17]. Indeed, the ESRF storage ring, which has started operation in 1992, will be upgraded until 2020 into a close-to 4th generation SR-source by a change of its magnetic lattice (ESRF II; dashed curve in (Figure 1A) [18]. Several other major 3rd generation SR sources (e.g. APS and SPring8) will follow this example. This will favor in particular “brilliancehungry” experimental techniques, currently proposed only at few SR beamlines worldwide. Examples are sub-μm SR-MPX [19, 20] (e.g. ID13ESRF); (Figure 2B) and time-resolved SRMPX based on picoseconds X-ray flashes using an undulator harmonics (“pink” beam), a technique currently developed only for larger SR beam foci [21]. One can estimate that a “pink” SR-MPX beam line would reach at ESRF-II the 1016 flux density range.

Synchrotron Radiation Serial Crystallography (SSX)

SSX on cryo frozen samples is becoming an automated data collection workflow at SR-MPX beam lines [22]. It has first been demonstrated for Trypanosoma brucei procathepsin B (TbCatB) crystallites of about 2 μm average size using helical raster-rotation scans to obtain “classical” rotation patterns and distribute the radiation dose (Figure 3A) [13]. The hits are displayed in a “heat map” scaled to the overall diffraction strength in each pattern (Figure 3B). The 0.3 nm resolution structure based on 426 patterns from 80 crystallites is of similar quality for the main-chain features as the 0.21 nm resolution SFX study based on 2.9x105 patterns [23].

The statistical treatment of SSX data based on the hierarchical cluster analysis [24] allows readily matching complementary patterns from many different crystallites into groups [25]. A potential target for this approach is exploring experimentally the mosaic block (called here: microdomain) model (Figure 4A) [26]. We note that individual micro-domains in the bulk of a well-ordered protein crystal are not readily accessible to a diffraction experiment. The combination of laser-microdissection and solvent-induced micro-fragmentation allows, however, physically separating a crystal into micro-domains as shown for a lysozyme crystal generated by the Langmuir-Blodgett nanotemplate technique (Figure 4B, 4C) [19, 27]. A raster-scan heat map obtained with a 400 nm beam of a micro-fragmented lysozyme crystal in a cryogenic loop revealed two micro-domains [figure 4D]. Rotation patterns were collected from each micro-domain and their 3D structures refined [19].The results suggest that laser-induced microcavitation and solvent-induced microdomain separation do not introduce lattice distortions. SSX of a sufficiently large set of micro-domains from a microfragmented crystal could possibly provide information on the variability of crystallographic parameters or allow picking out crystalline micro-domains for highly mosaic crystals.

SSX at room temperature is a challenge for SR-MPX due to radiation damage effects although secondary radiation damage becomes negligible for crystallites in the μm-range [28, 29]. A number of room temperature sample environments tested at SR-MPX beam lines have been initially developed for SFX experiments [12, 30-33]. Such experiments are generally performed without crystal rotation. Probing a capillary filled with a lysozyme crystallite flush [34] would, however, not be possible at an XFEL due to an immediate destruction of the capillary walls. The SSX lysozyme structure was refined to 0.21 nm based on about 4x104 patterns using about 250 mg protein. Increasing the flow-density by a liquid crystalline polymer (LCP) phase allows reducing the protein consumption to the 1 mg range. Indeed, an LCP matrix filled with about 30 μm size bacteriorhodopsin crystallites was extruded into air and probed by SSX [35].This membrane protein structure was refined to 0.24 nm resolution. A similar protein consumption has been obtained for randomly distributed crystallites on a fixed target by raster-scan SFX [32]. The same approach was used for SSX with micro- and nanobeams on a slurry of lysozyme crystallites contained between Si3N4 membranes (Figure 5A, 5B). The main-chain lysozyme structure was only slightly affected by radiation damage and there was practically no difference for the two beam sizes. The particularly high radiation dose for nanobeam SSX of 29 MGy/crystallite was tentatively attributed to a lag phase [20].The availability of up to KHz framing rate, zero readout noise pixel detectors -such as the EIGER detector from DECTRIS®- will allow further reducing protein consumption in SSX experiments.

On-Chip Sample Environments and Low Contact-Force Manipulation

Sample environments for SX experiments have to cope with the manipulation of μm- to nm-sized biological objects which suggests exploring the use of nanobiotechnology tools and techniques. Furthermore, deterministic positioning of objects in the beam allows reducing the sample consumption and therefore also the data collection time by increasing the crystallites hit rate. The fragility of many proteins, such as membrane proteins, also requires manipulation and positioning with low contact forces. Ideally, self-assembly into crystalline objects and their localization should be done in the same sample environment. The strategies discussed below are likewise of interest for SFX and SSX. A more detailed overview on different positioning & manipulation techniques will be provided elsewhere [36].

Sorting of objects on structured substrates

The aim is to preposition objects on a structured surface so that a high hit rate can be obtained by mesh-scans with a step size corresponding to the separation of the objects. An example for this is provided by a silicon chip with a holepattern etched into a 10 μm membrane by photolithography techniques (Figure 6A) [37]. Evaporating a droplet containing a slush of crystallites on the chip allows immobilizing individual crystallites in the down to 1 μm diameter holes by capillary action (Figure 6B).

Chips with nanofabricated pillared superhydrophobic surfaces are an alternative possibility for exploiting localization of objects during droplet evaporation (Figure 6C, 6D) [38]. The shrinkage of a water or dilute solute droplet during evaporation results in a wetting transition with liquid entering the gaps between the pillars [38]. At higher solute concentrations, a viscous protein layer is formed at the droplet rim by convective-flow mediated mass transport during evaporation. The reduced molecular mobility at the rim can result in self-assembly and the formation of 1D or 2D morphologies [39, 40]. Indeed, a solution of rod-like tobacco mosaic virus (TMV) particles of 300 nm length and 18 nm diameter forms a coffee-ring type layer on the pillars (Figure 7A) [40, 42]. Raster-diffraction with a 170x130 nm2 beam reveals micro-domains on and between the pillars with the nanorods axes aligned more or less parallel to the rim and pillar surface (Figure 7B, 7C). Single crystalline features, already noted in a TMV microbeam study [43], are apparent in a pattern from the residue of the retracting layer on top of a pillar (Figure 7A, 7B). The best resolution of 1.6 nm obtained until now for a TMV coffee-ring residue [43] cannot yet compete with the 0.29 nm resolution obtained by X-ray fiber diffraction on much larger scattering volumes [44]. Improving the resolution of self-assembled TMV particles on artificially structured substrates will be an interesting challenge.

Manipulation and assembly of objects with ultralow contact forces

Objects from nm to several 10th of μm dimensions can be trapped by pN optical forces generated by milliwatts of visible laser light focused through a microscope objective onto the object, such as crystallites in a capillary (Figure 8A) [45, 49]. The optical field reduces random motion due to Brownian forces, allowing raster-scans of trapped objects by microPX techniques [48, 49]. The laser beam can be split holographically into multiple traps [46]. Indeed, an about 30 μm insulin crystal could be kept in a fixed position by three holographic traps and its radiation damage explored in-situ using a dedicated optical tweezers setup (Figure 8B) [49]. Radiation damage appeared only beyond about 50 ms local exposure suggesting that SSX based on raster-rotation scans would be feasible for larger microcrystals provided that the separation of the scan points is a few μm, i.e. corresponding to the range of secondary radiation damage due to X-ray induced photoelectrons [50].

Materials used for sample supports or confinement

In order to cope with objects of very low scattering power, sample supports and confining walls have to have ultralow background scattering and X-ray absorption. Indeed, scattering from a 10 μm single-crystalline silicon membrane [37] is very low for a transmission of ~97 % at λ~0.1 nm wavelength. The transmission is > 99.8% for a 1 μm thick Si3N4 membrane used in a superhydrophobic chip [41]. This material is, however, very fragile and future sample supports should rather be based on few atomic layers thick graphene which has virtually 100 % transmission and no background scattering [51].


“Pushing the limits of protein crystallography to smaller crystals and smaller beam sizes requires the integration of more and more nanotechnology into a MPX beam line and annex laboratories” [1]. The examples reviewed in this article with an emphasis for on-chip sample environments support this statement and suggest R&D opportunities related to nanobiotechnology tools and techniques.


Helpful discussions with A. Accardo, F. De Angelis and G. Marinaro (IIT-Genova), E. Pechkova (Genova University), C. Nicolini (Fondazione ELBA), M. Burghammer, A. Popov, S.C. Santucci (ESRF-Grenoble), J.P. Colletier and N. Coquelle (IBS-Grenoble) are gratefully acknowledged.


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*Correspondence to:

Dr. Christian Riekel
European Synchrotron Radiation Facility
Experiments Division
Complex Systems and Biomedical Sciences Group
B.P.220, F-38043 Grenoble Cedex, France
Tel: 003347688205
Fax: 003476882542

Received: September 14, 2015
Accepted: October 5, 2015
Published: October 9, 2015

Citation: Riekel C. 2015. Protein Micro-Crystallography: Nanotechnology Challenges Ahead. NanoWorld J 1(3): 73-78.

Copyright: © 2015 Riekel. This is an Open Access article distributed under the terms of the Creative Commons Attribution 4.0 International License (CC-BY) ( which permits commercial use, including reproduction, adaptation, and distribution of the article provided the original author and source are credited.

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