<i>Mtb</i>GlyRS and <i>Mtr</i>GlyRS purify predominantly as monomers.

<i>Mtb</i>GlyRS and <i>Mtr</i>GlyRS purify predominantly as monomers.

<p><b>(A)</b><i>Mtb</i>GlyRS purified using a HiLoad 26/600 Superdex 75 column runs mostly at 47.3 kDa. <b>(B)</b> <i>Mtr</i>GlyRS purified using a HiLoad 26/600 Superdex 200 column elutes with an apparent mass of 36.9 kDa.</p>

-д хадгалсан:

Номзүйн дэлгэрэнгүй
Үндсэн зохиолч:	Michael K. Fenwick (1663099) (author)
Бусад зохиолчид:	Amy E. DeRocher (698177) (author), Justin K. Craig (10687219) (author), Elizabeth K. Harmon (21627186) (author), Steve Seibold (9428067) (author), Lijun Liu (452265) (author), Kevin P. Battaile (418240) (author), Lynn K. Barrett (293068) (author), Wesley C. Van Voorhis (10332534) (author), Isabelle Q. Phan (17132106) (author), Bart L. Staker (244387) (author), Sandhya Subramanian (348582) (author), Scott Lovell (122251) (author), Peter J. Myler (244412) (author)
Хэвлэсэн:	2025
Нөхцлүүд:	Biophysics Biochemistry Molecular Biology Pharmacology Infectious Diseases Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various liganded states structurally characterized previously structural genomics pipeline size exclusion chromatography several liganded states prospective drug targets div >< p based drug discovery mycobacterium tuberculosis </ mycobacterium thermoresitibile </ mycobacterium thermoresistibile </ mycobacterium smegmatis </ escherichia coli </ dimeric state characteristic glyrs apoenzyme crystal glycyl trna synthetases mtr </ mtb </ trna synthetases apo state two enzymes significant portions recent work lid motif insertion domain human glyrs human enzyme glyrs ), dual targeted dimer interface despite crystallizing crystal structures adenosine monophosphate 95 å 85 å
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