2CY1

Crystal structure of APE1850

Summary for 2CY1

• Entry DOI: 10.2210/pdb2cy1/pdb
• Descriptor: NusA protein homolog (2 entities in total)
• Functional Keywords: transcription termination, rna binding protein, archaeal nusa, kh domain, microgravity, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transcription
• Biological source: Aeropyrum pernix
• Total number of polymer chains: 1
• Total formula weight: 16069.72

Authors

Shibata, R.,Bessho, Y.,Umehara, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-07-04, release date: 2006-01-04, Last modification date: 2023-10-25)

Primary citation

Tanaka, H.,Umehara, T.,Inaka, K.,Takahashi, S.,Shibata, R.,Bessho, Y.,Sato, M.,Sugiyama, S.,Fusatomi, E.,Terada, T.,Shirouzu, M.,Sano, S.,Motohara, M.,Kobayashi, T.,Tanaka, T.,Tanaka, A.,Yokoyama, S.
Crystallization of the archaeal transcription termination factor NusA: a significant decrease in twinning under microgravity conditions
Acta Crystallogr.,Sect.F, 63:69-73, 2007

PubMed Abstract: The transcription termination factor NusA from Aeropyrum pernix was crystallized using a counter-diffusion technique in both terrestrial and microgravity environments. Crystallization under microgravity conditions significantly reduced the twinning content (1.0%) compared with terrestrially grown crystals (18.3%) and improved the maximum resolution from 3.0 to 2.29 A, with similar unit-cell parameters. Based on a comparison of the crystal parameters, the effect of microgravity on protein crystallization is discussed.

PubMed: 17277442
DOI: 10.1107/S1744309106054625

Experimental method

X-RAY DIFFRACTION (2.3 Å)