New expression of bimodal phase distributions in direct-method phasing of protein single-wavelength anomalous diffraction data

One of the essential points of the direct-method single-wavelength anomalous diffraction （SAD） phasing for proteins is to express the bimodal SAD phase distribution by the sum of two Gaussian functions peaked respectively at φh″＋｜△φh｜ and φh″-｜△φh｜. The probability for △φh being positive （P＋） can be derived based on the Cochran distribution in direct methods. Hence the SAD phase ambiguity can be resolved by multiplying the Gaussian function peaked at φh″＋｜△φh｜ with P＋ and multiplying the Gaussian function peaked at φh″-｜△φh｜ with P_ （=1- P＋）. The direct-method SAD h phasing has been proved powerful in breaking SAD phase ambiguities, in particular when anomalous-scattering signals are weak. However, the approximation of bimodal phase distributions by the sum of two Gaussian functions introduces considerable errors. In this paper we show that a much better approximation can be achieved by replacing the two Gaussian functions with two von Mises distributions. Test results showed that this leads to significant improvement on the efficiency of direct-method SAD-phasing.

DSAS:A new macromolecular substructure solution program based on the modified phase-retrieval algorithm

Considering the pivotal role of single-wavelength anomalous diffraction(SAD) in macromolecular crystallography,our objective was to introduce DSAS,a novel program designed for efficient anomalous scattering substructure determination.DSAS stands out with its core components:a modified phase-retrieval algorithm and automated parameter tuning.The software boasts an intuitive graphical user interface(GUI),facilitating seamless input of essential data and real-time monitoring.Extensive testing on DSAS has involved diverse datasets,encompassing proteins,nucleic acids,and various anomalous scatters such as sulfur(S),selenium(Se),metals,and halogens.The results confirm DSAS’s exceptional performance in accurately determining heavy atom positions,making it a highly effective tool in the field.

Crystallographic Studies of Cephalosporin Acylase from Pseudomonas sp. Strain 130

The cephalosporin acylases are a group of enzymes that hydrolyze cephalosporin C and/or glutaryl 7 aminocephalosporanic acid to produce 7 aminocephalosporanic acid. The cephalosporin acylase from Pseudomonas sp. strain 130 was crystallized in two different forms suitable for structural studies. A tetragonal crystal form diffracted to 0.24 nm belonged to the space group P4 12 12. There was one αβ heterodimer per asymmetric unit. A second crystal form diffracted to 0.21 nm belonged to the space group P2 1. There was four αβ heterodimers per asymmetric unit. The tetragonal crystal structure of CA 130 was determined using the multiwavelength anomalous diffraction method and the P2 1 crystal structure was then determined using the molecular replacement method.