Literature DB >> 2678097

Single crystals of bacteriophage T7 RNA polymerase.

R Sousa1, J P Rose, Y J Chung, E M Lafer, B C Wang.   

Abstract

Single crystals of T7 RNA polymerase have been grown to a maximum size of 1.8 x 0.3 x 0.3 mm. The crystals are composed of fully intact T7 RNA polymerase which is enzymatically active upon dissolution. These crystals belong to the monoclinic space group P2(1) and have unit cell parameters a = 114.5 A, b = 139.6 A, c = 125.7 A, and beta = 98.1 degrees. Self-rotation function studies indicate that there are three molecules per asymmetric unit. The crystals diffract to at least 3.0 A resolution. These are the first crystals of a DNA-dependent RNA polymerase suitable for high-resolution X-ray structure determination.

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Year:  1989        PMID: 2678097     DOI: 10.1002/prot.340050403

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  2 in total

1.  Bacterial RNA polymerases: structural and functional relationships.

Authors:  R E Glass; R S Hayward
Journal:  World J Microbiol Biotechnol       Date:  1993-07       Impact factor: 3.312

2.  Mutations in T7 RNA polymerase that support the proposal for a common polymerase active site structure.

Authors:  G Bonner; D Patra; E M Lafer; R Sousa
Journal:  EMBO J       Date:  1992-10       Impact factor: 11.598

  2 in total

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