Small angle neutron scattering (SANS) provides a method to obtain important low-resolution information for integral membrane proteins (IMPs), challenging targets for structural determination. Specific deuteration furnishes a "stealth" carrier for the solubilized IMP. We used SANS to determine a structural envelope of SpNOX, the Streptococcus pneumoniae NADPH oxidase (NOX), a prokaryotic model system for exploring structure and function of eukaryotic NOXes. SpNOX was solubilized in the detergent lauryl maltose neopentyl glycol, which provides optimal SpNOX stability and activity. Using deuterated solvent and protein, the lauryl maltose neopentyl glycol was experimentally undetected in SANS. This affords a cost-effective SANS approach for obtaining novel structural information on IMPs. Combining SANS data with molecular modeling provided a first, to our knowledge, structural characterization of an entire NOX enzyme. It revealed a distinctly less compact structure than that predicted from the docking of homologous crystal structures of the separate transmembrane and dehydrogenase domains, consistent with a flexible linker connecting the two domains.

中文翻译：

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SANS 建议使用 LMNG 隐形载体在 NADPH 氧化酶内的域间灵活性。

小角度中子散射 (SANS) 提供了一种获得重要的低分辨率信息的方法，用于整合膜蛋白 (IMP)，具有挑战性的结构测定目标。特定的氘化为溶解的 IMP 提供了“隐形”载体。我们使用 SANS 来确定 SpNOX、肺炎链球菌 NADPH 氧化酶 (NOX) 的结构包膜，这是一种用于探索真核 NOX 结构和功能的原核模型系统。SpNOX 溶解在洗涤剂月桂基麦芽糖新戊二醇中，可提供最佳的 SpNOX 稳定性和活性。使用氘代溶剂和蛋白质，月桂基麦芽糖新戊二醇在 SANS 中未通过实验检测到。这提供了一种具有成本效益的 SANS 方法，用于获取有关 IMP 的新结构信息。据我们所知，将 SANS 数据与分子建模相结合，提供了第一个完整 NOX 酶的结构表征。它揭示了一个明显不如从独立跨膜和脱氢酶域的同源晶体结构对接预测的结构紧凑，与连接两个域的灵活接头一致。