Of course not, as I know you know. I'm also guessing you saw the recent breakthroughs on cryogenic electron microscopy and its application to being able to essentially "see" down to just about the molecular level for the proteins, potentially obviating the need to grow pure single crystals of proteins and even small molecules in order to determine structure, which historically has been done via X-ray diffraction patterns on such crystals. Derek Lowe posted on this yesterday on his blog, linked below, as two breakthrough papers on this technology were just published in Nature.
Crystals are very precisely ordered/arranged and the diffraction pattern can be analyzed via software to determine exactly how molecules are connected and crystals are usually fairly easy to isolate for small molecules (although not always - I've done a ton of work in the field of crystallography and have 2 patents in this area). However, it's often extremely hard to grow pure crystals of biological molecules like proteins, so their structure can be elucidated by X-rays. But with cryo electron microscopy, it may not always be necessary any more as this technology can elucidate 3-D structure directly (via very advanced software).
https://blogs.sciencemag.org/pipeline/archives/2020/10/30/down-to-the-atoms
https://www.nature.com/articles/s41586-020-2829-0
https://www.nature.com/articles/s41586-020-2833-4
In addition, this technology has been put to work to help elucidate some of the structural elements of the proteins on the SARS-CoV-2 virus and how they interact with various human proteins - in particular the peptidases of the angiotensin-converting enzyme 2 (ACE2), which the virus "mates with" via its spike proteins to gain entry into various epithelial cells in the lungs and blood vessels and elsewhere. The graphic below shows the outcome of some of this work - pretty cool stuff.
https://directorsblog.nih.gov/tag/cryo-em/