Purification, crystallization, and preliminary X-ray studies of 10-formyltetrahydrofolate synthetase from Clostridia acidici-urici

✍ Scribed by Linda D'Ari; Edwin Cheung; Jesse C. Rabinowitz; Jill M. Bolduc; Jie-Yu Huang; Barry L. Stoddard

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 59 KB
• Volume: 27
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199702)27:2<319::aid-prot18>3.0.co;2-p

✦ Synopsis

The monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and crystallized. The crystals belong to space group P2 1 , with unit cell dimensions a 5 102.4 Å, b 5 116.5 Å, c 5 115.8 Å, and b 5 103.5. The crystal unit cell and diffraction is consistent with an asymmetric unit consisting of the enzyme tetramer, and a specific volume of the unit cell of 2.7 Å 3 /Da. The crystals diffract to at least 2.3 Å resolution after flash-cooling, when using a rotating anode x-ray source and an RAXIS image plate detector.