Publication Abstract from PubMed
Carboxypeptidase 1 from the thermophilic eubacterium Thermus thermophilus (TthCP1, 58 kDa), a member of the M32 family of metallocarboxypeptidases, was crystallized by the sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals diffracted X-rays to beyond 2.6 A resolution using a synchrotron-radiation source. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 171.0, b = 231.6, c = 124.9 A. The crystal contains three molecules in an asymmetric unit (VM = 2.11 A3 Da(-1)) and has a solvent content of 61.5%.
Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.,Nagata K, Tsutsui S, Lee WC, Ito K, Kamo M, Inoue Y, Tanokura M Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1445-6. Epub 2004, Jul 21. PMID:15272172[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
