Crystallography Research Today is a free monthly online journal that collates and summarizes the latest research about Crystallography, including details on x-ray crystals, techniques, analyses, structures.

Single mimivirus particles intercepted and imaged with an X-ray laser.

Seibert MM, Ekeberg T, Maia FR, Svenda M, Andreasson J, Jönsson O, Odić D, Iwan B, Rocker A, Westphal D, Hantke M, DePonte DP, Barty A, Schulz J, Gumprecht L, Coppola N, Aquila A, Liang M, White TA, Martin A, Caleman C, Stern S, Abergel C, Seltzer V, Claverie JM, Bostedt C, Bozek JD, Boutet S, Miahnahri AA, Messerschmidt M, Krzywinski J, Williams G, Hodgson KO, Bogan MJ, Hampton CY, Sierra RG, Starodub D, Andersson I, Bajt S, Barthelmess M, Spence JC, Fromme P, Weierstall U, Kirian R, Hunter M, Doak RB, Marchesini S, Hau-Riege SP, Frank M, Shoeman RL, Lomb L, Epp SW, Hartmann R, Rolles D, Rudenko A, Schmidt C, Foucar L, Kimmel N, Holl P, Rudek B, Erk B, Hömke A, Reich C, Pietschner D, Weidenspointner G, Strüder L, Hauser G, Gorke H, Ullrich J, Schlichting I, Herrmann S, Schaller G, Schopper F, Soltau H, Kühnel KU, Andritschke R, Schröter CD, Krasniqi F, Bott M, Schorb S, Rupp D, Adolph M, Gorkhover T, Hirsemann H, Potdevin G, Graafsma H, Nilsson B, Chapman HN, Hajdu J

Laboratory of Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Husargatan 3, SE-751 24 Uppsala, Sweden.

X-ray lasers offer new capabilities in understanding the structure of biological systems, complex materials and matter under extreme conditions. Very short and extremely bright, coherent X-ray pulses can be used to outrun key damage processes and obtain a single diffraction pattern from a large macromolecule, a virus or a cell before the sample explodes and turns into plasma. The continuous diffraction pattern of non-crystalline objects permits oversampling and direct phase retrieval. Here we show that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source. Calculations indicate that the energy deposited into the virus by the pulse heated the particle to over 100,000 K after the pulse had left the sample. The reconstructed exit wavefront (image) yielded 32-nm full-period resolution in a single exposure and showed no measurable damage. The reconstruction indicates inhomogeneous arrangement of dense material inside the virion. We expect that significantly higher resolutions will be achieved in such experiments with shorter and brighter photon pulses focused to a smaller area. The resolution in such experiments can be further extended for samples available in multiple identical copies.

Published 4 February 2011 in Nature, 470(7332): 78-81.
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Articles on Crystallography published 4 February 2011:

Single mimivirus particles intercepted and imaged with an X-ray laser.   Nature, 470(7332): 78-81.

X-ray lasers offer new capabilities in understanding the structure of biological systems, complex materials and matter under extreme conditions. Very short and extremely bright, coherent X-ray pulses can be used to outrun key damage processes and obtain a single diffraction pattern from a large macromolecule, a virus or a cell before the sample explodes and turns into plasma. The continuous diffraction pattern of non-crystalline objects permits oversampling and direct phase retrieval. Here we ... [Abstract] [Full-text]

Femtosecond X-ray protein nanocrystallography.   Nature, 470(7332): 73-7.

X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been ... [Abstract] [Full-text]

Femtosecond X-ray protein nanocrystallography.   Nature, 470(7332): 73-7.

X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded. It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been ... [Abstract] [Full-text]

Articles on Crystallography published 24 November 2010:

Structure of N-(5-ethyl-[1,3,4]-thiadiazole-2-yl)toluenesulfonamide by combined X-ray powder diffraction, 13C solid-state NMR and molecular modelling.   Acta Crystallogr B, 66: 615-21.

The crystal structure solution of the title compound is determined from microcrystalline powder using a multi-technique approach that combines X-ray powder diffraction (XRPD) data analysis based on direct-space methods with information from (13)C solid-state NMR (SSNMR), and molecular modelling using the GIPAW (gauge including projector augmented-wave) method. The space group is Pbca with one molecule in the asymmetric unit. The proposed methodology proves very useful for unambiguously ... [Abstract] [Full-text]

Articles on Crystallography published 27 October 2010:

An X-ray diffraction study of model membrane raft structures.   FEBS J, 277(22): 4685-98.

Protein sorting and assembly in membrane biogenesis and function involves the creation of ordered domains of lipids known as membrane rafts. The rafts are comprised of all the major classes of lipids, including glycerophospholipids, sphingolipids and sterol. Cholesterol is known to interact with sphingomyelin to form a liquid-ordered bilayer phase. Domains formed by sphingomyelin and cholesterol, however, represent relatively small proportions of the lipids found in membrane rafts and the ... [Abstract] [Full-text]

An X-ray diffraction study of model membrane raft structures.   FEBS J, 277(22): 4685-98.

Protein sorting and assembly in membrane biogenesis and function involves the creation of ordered domains of lipids known as membrane rafts. The rafts are comprised of all the major classes of lipids, including glycerophospholipids, sphingolipids and sterol. Cholesterol is known to interact with sphingomyelin to form a liquid-ordered bilayer phase. Domains formed by sphingomyelin and cholesterol, however, represent relatively small proportions of the lipids found in membrane rafts and the ... [Abstract] [Full-text]

Articles on Crystallography published 25 October 2010:

Crystal structures of phosphoketolase: thiamine diphosphate-dependent dehydration mechanism.   J Biol Chem, 285(44): 34279-87.

Thiamine diphosphate (ThDP)-dependent enzymes are ubiquitously present in all organisms and catalyze essential reactions in various metabolic pathways. ThDP-dependent phosphoketolase plays key roles in the central metabolism of heterofermentative bacteria and in the pentose catabolism of various microbes. In particular, bifidobacteria, representatives of beneficial commensal bacteria, have an effective glycolytic pathway called bifid shunt in which 2.5 mol of ATP are produced per glucose. ... [Abstract] [Full-text]

Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI.   J Biol Chem, 285(44): 33764-70.

Collagen and fibronectin (FN) are two abundant and essential components of the vertebrate extracellular matrix; they interact directly with cellular receptors and affect cell adhesion and migration. Past studies identified a FN fragment comprising six modules, (6)FnI(1-2)FnII(7-9)FnI, and termed the gelatin binding domain (GBD) as responsible for collagen interaction. Recently, we showed that the GBD binds tightly to a specific site within type I collagen and determined the structure of domains ... [Abstract] [Full-text]

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