Abstract:
:Crystals of Proteus vulgaris holotryptophanase have been grown by the hanging-drop technique using polyethylene glycol 4000 as precipitant in the presence of monovalent cations K+ or Cs+. Orthorhombic crystals (P2(1)2(1)2(1)) grown with Cs+ have unit cell parameters a = 115.0 A, b = 118.2 A and c = 153.7 A and diffract to 1.8 A. There are four subunits of the tetrameric molecule in the asymmetric unit. Native data have been collected to 2.5 A resolution. The 3.4 A data were collected from tetragonal crystals of Escherichia coli holotryptophanase grown under conditions described by Kawata et al. (1991). The molecular replacement solution for this crystal form has been found using tyrosine phenol-lyase coordinates. The correct enantiomorph is P4(3)2(1)2. There are two subunits in the asymmetric unit.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Dementieva IS,Zakomirdina LN,Sinitzina NI,Antson AA,Wilson KS,Isupov MN,Lebedev AA,Harutyunyan EHdoi
10.1006/jmbi.1994.1033subject
Has Abstractpub_date
1994-01-14 00:00:00pages
783-6issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(84)71033-3journal_volume
235pub_type
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