Guide to serial synchrotron crystallography

Nam, Ki Hyun

doi:10.1016/j.crstbi.2024.100131

Cited by 4 publications

(2 citation statements)

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“…Serial crystallography (SX), which employs an X-ray-free electron laser or a synchrotron X-ray, is an experimental technique that can determine the room temperature structure while minimizing the radiation damage [25][26][27]. During an SX experiment, a large number of crystal samples are delivered to the X-ray interaction point and exposed to the X-ray only once.…”

Section: Introductionmentioning

confidence: 99%

Comparative Analysis of Room Temperature Structures Determined by Macromolecular and Serial Crystallography

Nam

2024

Crystals

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Temperature directly influences the function and structure of proteins. Crystal structures determined at room temperature offer more biologically relevant structural information regarding flexibility, rigidity, and thermal motion than those determined by conventional cryocrystallography. Crystal structures can be determined at room temperature using conventional macromolecular crystallography (MX) or serial crystallography (SX) techniques. Among these, MX may theoretically be affected by radiation damage or X-ray heating, potentially resulting in differences between the room temperature structures determined by MX and SX, but this has not been fully elucidated. In this study, the room temperature structure of xylanase GH11 from Thermoanaerobacterium saccharolyticum was determined by MX (RT-TsaGH11-MX). The RT-TsaGH11-MX exhibited both the open and closed conformations of the substrate-binding cleft within the β-sandwich fold. The RT-TsaGH11-MX showed distinct structural changes and molecular flexibility when compared with the RT-TsaGH11 determined via serial synchrotron crystallography. The notable molecular conformation and flexibility of the RT-TsaGH11-MX may be induced by radiation damage and X-ray heating. These findings will broaden our understanding of the potential limitations of room temperature structures determined by MX.

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Section: Introductionmentioning

confidence: 99%

Comparative Analysis of Room Temperature Structures Determined by Macromolecular and Serial Crystallography

Nam

2024

Crystals

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“…As a result, TR-SX allows to obtain structural dynamics information and observe biological macromolecules in action by capturing transient intermediates along a biological pathway. [3][4][5][6] From an experimental point of view, serial crystallography brings new constraints on crystal preparation as it intrinsically requires a large amount of samples to make sure to collect a complete diffraction data set. Moreover optimal time-resolved experiments require crystalline samples with a narrow size distribution in order to ensure a uniform triggering of the reaction under study through the entire crystal volume.…”

Section: ■ Introductionmentioning

confidence: 99%

The nucleating agent crystallophore induces instant protein crystallization

Sauter,

Housset,

Orlans

et al. 2024

Preprint

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The rapid preparation of homogeneous suspensions of micro- or nano-crystals is a crucial step in serial crystallography. We show how additives, such as the crystallophore (TbXo4) that acts as a molecular glue by promoting protein-protein interactions, can facilitate sample preparation for both serial synchrotron crystallography (SSX) and micro electron diffraction (3D ED). This lanthanide complex was used here for its nucleating properties to crystallize hen egg white lysozyme. SAXS monitoring indicates that crystals formed in a few minutes in low salt conditions that would not lead to spontaneous nucleation. Resulting micro- and nano-crystals were successfully used to determine the structure of the lysozyme-TbXo4 complex by SSX and 3D ED, illustrating the diffraction quality of the produced crystals and the usefulness of such compounds in the sample preparation pipeline for serial crystallography.

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Temperature-dependent structural changes in xylanase II from Trichoderma longibrachiatum

Nam

2024

Carbohydrate Research

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Guide to serial synchrotron crystallography

Cited by 4 publications

References 50 publications

Comparative Analysis of Room Temperature Structures Determined by Macromolecular and Serial Crystallography

Comparative Analysis of Room Temperature Structures Determined by Macromolecular and Serial Crystallography

The nucleating agent crystallophore induces instant protein crystallization

Temperature-dependent structural changes in xylanase II from Trichoderma longibrachiatum

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