Crystallization of ApoA1 and ApoE4 Nanolipoprotein Particles and Initial XFEL-Based Structural Studies

Shelby, Megan; Gilbile, Deepshika; Grant, Thomas D.; Bauer, William; Segelke, Brent; He, Wei; Evans, Angela C.; Crespo, Natalia; Fischer, Pontus; Pakendorf, Tim; Hennicke, Vincent; Hunter, Mark S.; Batyuk, Alex; Barthelmess, Miriam; Meents, Alke; Kuhl, Tonya L.; Frank, Matthias; Coleman, Matthew A.

doi:10.3390/cryst10100886

Title: Crystallization of ApoA1 and ApoE4 Nanolipoprotein Particles and Initial XFEL-Based Structural Studies

Journal Article · Thu Oct 01 00:00:00 EDT 2020 · Crystals

DOI:https://doi.org/10.3390/cryst10100886· OSTI ID:1770133

Shelby, Megan ^[1];

^[2];

^[3]; Bauer, William ^[4]; Segelke, Brent ^[1];

^[1]; Evans, Angela C. ^[5]; Crespo, Natalia ^[3];

^[6]; Pakendorf, Tim ^[6];

^[6]; Hunter, Mark S. ^[7]; Batyuk, Alex ^[7]; Barthelmess, Miriam ^[6]; Meents, Alke ^[6];

^[2];

^[5];

^[5]

Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
Univ. of California, Davis, CA (United States)
State Univ. of New York (SUNY), Buffalo, NY (United States); Hauptman-Woodward Medical Research Inst., Buffalo, NY (United States)
Hauptman-Woodward Medical Research Inst., Buffalo, NY (United States)
Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States); Univ. of California at Davis, Sacramento, CA (United States)
Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
SLAC National Accelerator Lab., Menlo Park, CA (United States)

Nanolipoprotein particles (NLPs), also called “nanodiscs”, are discoidal particles with a patch of lipid bilayer corralled by apolipoproteins. NLPs have long been of interest due to both their utility as membrane-model systems into which membrane proteins can be inserted and solubilized and their physiological role in lipid and cholesterol transport via high-density lipoprotein (HDL) and low-density lipoprotein (LDL) maturation, which are important for human health. Serial femtosecond crystallography (SFX) at X-ray free electron lasers (XFELs) is a powerful approach for structural biology of membrane proteins, which are traditionally difficult to crystallize as large single crystals capable of producing high-quality diffraction suitable for structure determination. To facilitate understanding of the specific role of two apolipoprotein/lipid complexes, ApoA1 and ApoE4, in lipid binding and HDL/LDL particle maturation dynamics, and to develop new SFX methods involving NLP membrane protein encapsulation, we have prepared and crystallized homogeneous populations of ApoA1 and ApoE4 NLPs. Crystallization of empty NLPs yields semi-ordered objects that appear crystalline and give highly anisotropic and diffuse X-ray diffraction, similar to fiber diffraction. Several unit cell parameters were approximately determined for both NLPs from these measurements. Thus, low-background, sample conservative methods of delivery are critical. Here we implemented a fixed target sample delivery scheme utilizing the Roadrunner fast-scanning system and ultra-thin polymer/graphene support films, providing a low-volume, low-background approach to membrane protein SFX. This study represents initial steps in obtaining structural information for ApoA1 and ApoE4 NLPs and developing this system as a supporting scaffold for future structural studies of membrane proteins crystalized in a native lipid environment.

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Research Organization:: SLAC National Accelerator Lab., Menlo Park, CA (United States); Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); National Science Foundation (NSF); USDOE National Nuclear Security Administration (NNSA)

Grant/Contract Number:: AC02-76SF00515; 1R01GM117342; U19AI144184; STC-1231306; AC52-07NA27344

OSTI ID:: 1770133

Alternate ID(s):: OSTI ID: 1860863

Report Number(s):: LLNL-JRNL-814942; TRN: US2206796

Journal Information:: Crystals, Vol. 10, Issue 10; ISSN 2073-4352

Publisher:: MDPICopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
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lipoprotein
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serial femtosecond crystallography
XFELs
fixed target delivery

Title: Crystallization of ApoA1 and ApoE4 Nanolipoprotein Particles and Initial XFEL-Based Structural Studies

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