## 1 Introduction  
Macromolecular crystallography (MX) enables the determination of macromolecule crystal structures at atomic resolutions [1]. Such structural information provides useful information for understanding the molecular mechanisms of macromolecules [2, 3, 4] and provides insights into new drug design [5, 6] and rational protein engineering for industrial and medical applications [7, 8]. However, despite these advantages, radiation damage due to the absorption of X-ray radiation by crystals remains a major obstacle for MX [9]. When macromolecule crystals are absorbed the X-rays, free radicals are generated in the crystal [10, 11] that propagate global or specific radiation damage [12]. In global radiation damage, an overall increase in nonisomorphism in the crystal weakens the diffraction intensity of the crystal, lowers the resolution, increases the volume of the unit cell, and increases the Wilson B coefficient [11, 13]. Specific radiation damage affects the electron density map, such as elongation and breakage of disulfide bond sites, decarboxylation of aspartic acid and glutamic acid side chains, disorganization of methionine sulfur, and photoreduction of metal centers [11, 13, 14, 15, 16, 17, 18]. Accordingly, radiation damage reduces the diffraction data quality, disrupts experimental phasing, generates inaccuracy of the solved structure, and results in unreliable biological structures [19, 20, 21]. The focal size achievable in low-emittance third-generation synchrotron sources is reducing [22]. In particular, it is now possible to focus X-rays to a size of several \(\upmu\)m using optical devices such as KB mirrors [23], providing a very high flux density to the sample. These intense X-rays provide a strong signal to collect improved diffraction, absorption, and scattering data. However, when these intense X-rays is continuously exposed to the sample, radiation damage can be caused. To reduce the radiation damage on crystal sample, various attempts have been made to understand radiation damage theoretically and experimentally in MX [9; 10; 14; 24; 25; 26; 27; 28; 29]. Thaumatin is a plant sweet protein that contains eight disulfide bonds [30]. This protein is often used as a model crystal sample for radiation damage in MX experiments [22; 31; 32]. For example, [PERSON] et al. investigated beam-size effects in radiation damage to thaumatin crystals [22]. X-rays (photons/s = 0.75 \(\times\) 10\({}^{12}\)) of 82 \(\times\) 10 \(\upmu\)m (h x v) and 85 \(\times\) 170 \(\upmu\)m size were exposed to thaumatin I (300 \(\times\) 150 \(\times\) 100 \(\upmu\)m\({}^{3}\)) and thaumatin II (350 \(\times\) 150 \(\times\) 150 \(\upmu\)m\({}^{3}\)), respectively, to investigate the radiation damage for each beam size; a negative electron density of disulfide bond Cys159-Cys164 was observed. However, analysis of radiation damage to all disulfide bond sites in thaumatin has not been reported. In addition, because the specific and global radiation damage of crystals differ depending on the X-ray characteristics and collection strategy used, the results of previous studies cannot be applied to all experiments. Accordingly, Bragg peaks and structure analyses according to radiation damage in various data collection scenarios are important for optimal data collection utilization. Among them, research on data quality or radiation damage by using large crystals and a microfocusing beamline of \(<\)10 \(\upmu\)m is not well known. Theoretically, for single-point data collection, a part of the sample is continuously exposed to X-rays; therefore, multipoint or helical data collection strategies are useful for minimizing X-ray exposure of the same crystal volume [33]. However, it is not applicable on beamlines, unless multipoint or helical data collection is supported. In addition, there may be cases where single-point data collection is inevitably performed depending on the shape of the crystal or the shape of the mounted crystal.