Publications by authors named "Krishna Khakurel"

Crystallography has been the routine technique for studying high-resolution structures of proteins for over five decades. A major bottleneck in structure determination of macromolecules is obtaining crystals of a size and quality suitable for single-crystal X-ray crystallography experiments. Many challenging proteins either fail to grow into crystals or fail to grow into crystals of a size suitable for obtaining high-resolution structures using conventional X-ray crystallography.

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We report the first application of broadband time-resolved pump-probe ellipsometry to study the ultrafast dynamics of the photoinduced insulator-to-metal transition (IMT) in vanadium dioxide (VO) thin films driven by 35 fs laser pulses. This novel technique enables the direct measurement of the time-resolved evolution of the complex pseudodielectric function of VO during the IMT. We have identified distinct thermal and nonthermal dynamics in the photoinduced IMT, which critically depends on the pump wavelength and fluence, while providing a detailed temporal and spectral phase map.

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With the emergence of ultrafast X-ray sources, interest in following fast processes in small molecules and macromolecules has increased. Most of the current research into ultrafast structural dynamics of macromolecules uses X-ray free-electron lasers. In parallel, small-scale laboratory-based laser-driven ultrafast X-ray sources are emerging.

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X-ray crystallography is an established tool to probe the structure of macromolecules with atomic resolution. Compared with alternative techniques such as single-particle cryo-electron microscopy and micro-electron diffraction, X-ray crystallography is uniquely suited to room-temperature studies and for obtaining a detailed picture of macromolecules subjected to an external electric field (EEF). The impact of an EEF on proteins has been extensively explored through single-crystal X-ray crystallography, which works well with larger high-quality protein crystals.

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Electron crystallography of sub-micrometre-sized 3D protein crystals has emerged recently as a valuable field of structural biology. crystallization methods, utilizing lipidic mesophases, particularly lipidic cubic phases (LCPs), can produce high-quality 3D crystals of membrane proteins (MPs). A major step towards realizing 3D electron crystallography of MP crystals, grown , is to demonstrate electron diffraction from such crystals.

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A new modification of a table-top laser-driven water-jet plasma X-ray source has been successfully implemented and commissioned at the Extreme Light Infrastructure (ELI) Beamlines user facility. In order to preserve the broadband nature of the source for spectroscopic experiments, a polycapillary lens was initially chosen as the focusing element. Generally, polycapillary X-ray optics have a narrow photon acceptance angle and small field of view, making alignment complicated and time-consuming.

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The THz-field-driven streak camera has proven to be a powerful diagnostic-technique that enables the shot-to-shot characterization of the duration and the arrival time jitter of free electron laser (FEL) pulses. Here we investigate the performance of three computational approaches capable to determine the duration of FEL pulses with complex temporal structures from single-shot measurements of up to three simultaneously recorded spectra. We use numerically simulated FEL pulses in order to validate the accuracy of the pulse length retrieval in average as well as in a single-shot mode.

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Crystallography has long been the unrivaled method that can provide the atomistic structural models of macromolecules, using either X-rays or electrons as probes. The methodology has gone through several revolutionary periods, driven by the development of new sources, detectors, and other instrumentation. Novel sources of both X-ray and electrons are constantly emerging.

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The development of nanomedicines for the treatment of neurodegenerative disorders demands innovative nanoarchitectures for combined loading of multiple neuroprotective compounds. We report dual-drug loaded monoolein-based liquid crystalline architectures designed for the encapsulation of a therapeutic protein and a small molecule antioxidant. Catalase (CAT) is chosen as a metalloprotein, which provides enzymatic defense against oxidative stress caused by reactive oxygen species (ROS) such as hydrogen peroxide (HO).

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X-ray science has greatly benefited from the progress in X-ray optics. Advances in the design and the manufacturing techniques of X-ray optics are key to the success of various microscopic and spectroscopic techniques practiced today. Here the generation of apodized X-ray illumination using a two-stage deformable Kirkpatrick-Baez mirror system is presented.

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Unlike the electrostatic and electromagnetic lenses used in electron microscopy, most X-ray focusing optical systems have fixed optical parameters with constant numerical apertures (NAs). This lack of adaptability has significantly limited application targets. In the research described herein, we developed a variable-NA X-ray focusing system based on four deformable mirrors, two sets of Kirkpatrick-Baez-type focusing mirrors, in order to control the focusing size while keeping the position of the focus unchanged.

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Coherent diffraction imaging (CDI) is an established lensless imaging method widely used at the x-ray regime applicable to the imaging of non-periodic materials. Conventional CDI can practically image isolated objects only, which hinders the broader application of the method. We present the imaging of non-isolated objects by employing recently proposed "non-scanning" apodized-illumination CDI at an optical wavelength.

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