Nicusor Timneanu

Dr. Nicusor Timneanu

orcid

Research Focus & Metrics

Academic Career Length

29Years (1998-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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2 February 2011 in Nature
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HCHenry Chapman
Henry Chapman
PFPetra Fromme
Petra Fromme
ABAnton Barty
Anton Barty
TWThomas A. White
Thomas A. White
RKRichard A. Kirian
Richard A. Kirian
JSJohn C. H. Spence
John C. H. Spence

12 November 2006 in Nature Physics
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HCHenry Chapman
Henry Chapman
ABAnton Barty
Anton Barty
MBMichael J. Bogan
Michael J. Bogan
SBSébastien Boutet
Sébastien Boutet
MFMatthias Frank
Matthias Frank
JHJanos Hajdu
Janos Hajdu

20 July 2012 in Science
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Journal Article
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SBSébastien Boutet
Sébastien Boutet
LLLukas Lomb
Lukas Lomb
GWGarth J. Williams
Garth J. Williams
TBThomas R. M. Barends
Thomas R. M. Barends
AAAndrew Aquila
Andrew Aquila
ISIlme Schlichting
Ilme Schlichting
Size Matters Less: X-ray crystallography is a central research tool for uncovering the structures of proteins and other macromolecules. However, its applicability typically requires growth of large crystals, in part because a sufficient number of molecules must be present in the lattice for the sample to withstand x-ray—induced damage. Boutet et al. (p. 362 , published online 31 May) now demonstrate that the intense x-ray pulses emitted by a free-electron laser source can yield data in few enough exposures to uncover the high-resolution structure of microcrystals.

8 February 2006 in The Journal of Physical Chemistry B
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Journal Article
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DSDavid van der Spoel
David van der Spoel
PMPaul J. van Maaren
Paul J. van Maaren
PLPer Larsson
Per Larsson
NTNicusor Timneanu
Nicusor Timneanu

11 January 2013 in Science
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LRLars Redecke
Lars Redecke
KNKarol Nass
Karol Nass
DDDaniel P. DePonte
Daniel P. DePonte
TWThomas A. White
Thomas A. White
DRDirk Rehders
Dirk Rehders
HCHenry Chapman
Henry Chapman
Diffraction Before Destruction: A bottleneck in x-ray crystallography is the growth of well-ordered crystals large enough to obtain high-resolution diffraction data within an exposure that limits radiation damage. Serial femtosecond crystallography promises to overcome these constraints by using short intense pulses that out-run radiation damage. A stream of crystals is flowed across the free-electron beam and for each pulse, diffraction data is recorded from a single crystal before it is destroyed. Redecke et al. (p. 227 , published online 29 November; see the Perspective by Helliwell ) used this technique to determine the structure of an enzyme from Trypanosoma brucei , the parasite that causes sleeping sickness, from micron-sized crystals grown within insect cells. The structure shows how this enzyme, which is involved in degradation of host proteins, is natively inhibited prior to activation, which could help in the development of parasite-specific inhibitors.

15 April 2005 in Science
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ALA. M. Lindenberg
A. M. Lindenberg
JLJ. Larsson
J. Larsson
KSK. Sokolowski-Tinten
K. Sokolowski-Tinten
KGK. J. Gaffney
K. J. Gaffney
CBC. Blome
C. Blome
JHJ. B. Hastings
J. B. Hastings
The motion of atoms on interatomic potential energy surfaces is fundamental to the dynamics of liquids and solids. An accelerator-based source of femtosecond x-ray pulses allowed us to follow directly atomic displacements on an optically modified energy landscape, leading eventually to the transition from crystalline solid to disordered liquid. We show that, to first order in time, the dynamics are inertial, and we place constraints on the shape and curvature of the transition-state potential energy surface. Our measurements point toward analogies between this nonequilibrium phase transition and the short-time dynamics intrinsic to equilibrium liquids.