3IH2

TM1030 crystallized at 323K

Summary for 3IH2

• Entry DOI: 10.2210/pdb3ih2/pdb
• Related: 3IH3 3IH4
• Descriptor: Transcriptional regulator, TetR family (2 entities in total)
• Functional Keywords: tm1030, transcriptional regulator, temperature, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, dna-binding, transcription, transcription regulation, transcription regulator
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 24409.08

Authors

Koclega, K.D.,Chruszcz, M.,Bujacz, G.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2009-07-29, release date: 2009-08-11, Last modification date: 2023-11-22)

Primary citation

Koclega, K.D.,Chruszcz, M.,Zimmerman, M.D.,Bujacz, G.,Minor, W.
'Hot' macromolecular crystals.
Cryst.Growth Des., 10:580-586, 2010

PubMed Abstract: Transcriptional regulator protein TM1030 from the hyperthermophile Thermotoga maritima, as well as its complex with DNA, was crystallized at a wide range of temperatures. Crystallization plates were incubated at 4, 20, 37 and 50° C over 3 weeks. The best crystals of TM1030 in complex with DNA were obtained at 4, 20 and 37° C, while TM1030 alone crystallized almost equally well in all temperatures. The crystals grown at different temperatures were used for X-ray diffraction experiments and their structures were compared. Surprisingly, the models of TM1030 obtained from crystals grown at different temperatures are similar in quality. While there are some examples of structures of proteins grown at elevated temperatures in the PDB, these temperatures appear to be underrepresented. Our studies show that crystals of some proteins may be grown and are stable at broad range of temperatures. We suggest that crystallization experiments at elevated temperatures could be used as a standard part of the crystallization protocol.

PubMed: 20161694
DOI: 10.1021/cg900971h

Experimental method

X-RAY DIFFRACTION (2.3 Å)