Phasing at resolution higher than the experimental resolution

被引:57
|
作者
Caliandro, R
Carrozzini, B
Cascarano, GL
De Caro, L
Giacovazzo, C
Siliqi, D
机构
[1] CNR, Ist Cristallog, I-70126 Bari, Italy
[2] Univ Bari, Dipartimento Geomineral, I-70125 Bari, Italy
关键词
D O I
10.1107/S090744490500404X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Limited experimental resolution is a unavoidable feature in macromolecular crystallography: it may hinder or make difficult the determination of the crystal structure. A novel procedure is presented which from an approximate electron-density map extrapolates the moduli and phases of non-measured reflections beyond and behind the experimental resolution limit. Applications to a set of test structures show that the extrapolation can be successfully accomplished. As a consequence, the phase estimates of the observed reflections are subsequently improved and the interpretability of the corresponding electron-density map increases. The use of the extrapolated values for the non-measured reflections provides additional information for the map, which shows a resolution higher than the experimental resolution.
引用
收藏
页码:556 / 565
页数:10
相关论文
共 50 条
  • [1] Ab initio phasing at resolution higher than experimental resolution
    Caliandro, R
    Carrozzini, B
    Cascarano, GL
    De Caro, L
    Giacovazzo, C
    Siliqi, D
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2005, 61 : 1080 - 1087
  • [2] Phasing at Resolution higher than the Experimental one
    Caliandro, Rocco
    Carrozzini, Benedetta
    Cascarano, Giovanni L.
    De Caro, Liberato
    Giacovazzo, Carmelo
    Siliqi, Dritan
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2005, 61 : C83 - C83
  • [3] Phasing proteins at low resolution
    Andersson, KM
    Hovmoller, S
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 : 1174 - 1180
  • [4] Low-resolution phasing
    Podjarny, AD
    Urzhumtsev, AG
    MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 : 641 - 658
  • [5] Advantages of high-resolution phasing: MAD to atomic resolution
    Schmidt, A
    Gonzalez, A
    Morris, RJ
    Costabel, M
    Alzari, PM
    Lamzin, VS
    ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2002, 58 : 1433 - 1441
  • [6] ATOMIC RESOLUTION MAD PHASING.
    Gonzalez, A.
    Morris, R.
    Lamzin, V.
    Alzari, P.
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 1999, 55 : 211 - 212
  • [7] LOW RESOLUTION PHASING. ACHIEVEMENTS AND PERSPECTIVES
    Lunin, V. Y.
    Urzhumtsev, A. G.
    Podjarny, A. D.
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 1999, 55 : 121 - 121
  • [8] Density constraints and low-resolution phasing
    Urzhumtsev, AG
    Lunina, NL
    Skovoroda, TP
    Podjarny, AD
    Lunin, VY
    ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 : 1233 - 1244
  • [9] Ab initio protein phasing at 1.4 Å resolution
    Burla, MC
    Carrozzini, B
    Cascarano, GL
    De Caro, L
    Giacovazzo, C
    Polidori, G
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2003, 59 : 245 - 249
  • [10] Model based very low resolution phasing
    Podjarny, A
    Urzhumtsev, A
    Lunin, V
    DIRECT METHODS FOR SOLVING MACROMOLECULAR STRUCTURES, 1998, 507 : 421 - 431