title: Is single-wavelength anomalous scattering sufficient for solving phases? A comparison of different methods for a 2.1 A structure solution.
abstract: The structure of rusticyanin is the largest unknown structure (M(r) = 16.8 kDa) which has been recently solved by the direct-methods approach using only single-wavelength anomalous scattering (SAS) data from the native protein [Harvey et al. (1998). Acta Cryst. D54, 629-635]. Here, the results of the Sim distribution approach [Hendrickson & Teeter (1981). Nature (London), 290, 107-113] and of the CCP4 procedure MLPHARE [Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763] are compared with those from direct methods. Analysis against the final refined model shows that direct methods produced significantly better phases (average phase error 56 degrees ) and therefore significantly better electron-density maps than the Sim distribution and MLPHARE approaches (average phase error was around 63 degrees in both cases).
authors.affiliation: Institute of Physics, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
authors.forename: L
authors.initials: L
authors.lastname: Yu-dong
authors.forename: I
authors.initials: I
authors.lastname: Harvey
authors.forename: G
authors.initials: G
authors.lastname: Yuan-xin
authors.forename: Z
authors.initials: Z
authors.lastname: Chao-de
authors.forename: H
authors.initials: H
authors.lastname: Yi-zong
authors.forename: F
authors.initials: F
authors.lastname: Hai-fu
authors.forename: S S
authors.initials: SS
authors.lastname: Hasnain
authors.forename: Q
authors.initials: Q
authors.lastname: Hao
mesh_terms: D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray / Q000379:methods; D008432:Mathematical Computing; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions
chemical_list: D001426:Bacterial Proteins; D012996:Solutions; C012543:rusticyanin; D001400:Azurin