X-ray crystallography can be used to

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X-ray crystallography is a technique used in structural biology to reveal the three-dimensional arrangement of atoms within a crystallized molecule. 
Option 1: 'determine the three dimensional structure of a protien.' This is the correct purpose of X-ray crystallography: it provides detailed atomic coordinates that describe the 3D structure of the protein. The misspelling 'protiem' is a typographical issue, but the concept aligns with the method's goal. 
Option 2: 'determine the amino acid sequence of a protein.' Determining sequence is typically done by methods like Edman degradation or, more commonly now, mass spectrometry-based proteomics or DNA/RNA sequencing strategies for encoding genes; X-ray crystallography does not yield sequence information directly. 
Option 3: 'determine the nucleic acid sequence of a protein.' This option is conceptually flawed since nucleic acid sequences pertain to DNA or RNA, not proteins, and a protein product does not have a nucleic acid sequence. Moreover, crystallography focuses on the folded protein structure, not its nucleotide sequence. 
Option 4: 'determine the sturcture of a rotating anode X-ray generator.' This describes an X-ray source component, not a biological structure to be determined; crystallography uses X-ray diffraction data collected from crystals, not from characterizing the generator itself. 
In sum, among the choices, the one that aligns with the core application of X-ray crystallography is the determination of the three-dimensional structure of a protein, while the others describe sequence determination or instrument components rather than structural elucidation.

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X-ray crystallography can be used to

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