CRYSTALS OF A TERNARY COMPLEX OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 REVERSE-TRANSCRIPTASE WITH A MONOCLONAL-ANTIBODY FAB FRAGMENT AND DOUBLE-STRANDED DNA DIFFRACT X-RAYS TO 3.5-A RESOLUTION

被引:56
作者
JACOBOMOLINA, A
CLARK, AD
WILLIAMS, RL
NANNI, RG
CLARK, P
FERRIS, AL
HUGHES, SH
ARNOLD, E
机构
[1] RUTGERS STATE UNIV, DEPT CHEM, PISCATAWAY, NJ 08854 USA
[2] PROGRAM RESOURCES INC, FREDERICK, MD 21702 USA
[3] NCI, FREDERICK CANC RES & DEV CTR, BASIC RES PROGRAM, ADV BIOSCI LABS, FREDERICK, MD 21702 USA
关键词
ANTIBODY COCRYSTALLIZATION; DNA COCRYSTALLIZATION; AIDS; POLYMERASE STRUCTURE; PROTEIN NUCLEIC ACID INTERACTION;
D O I
10.1073/pnas.88.23.10895
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Two crystal forms of complexes have been grown that contain human immunodeficiency virus type 1 reverse transcriptase and a monoclonal antibody Fab fragment. One of the crystal forms (form II, space group P3(1)12, a = 168.7 angstrom, c = 220.3 angstrom) diffracts x-rays to 3.5-angstrom resolution and appears suitable for moderate-resolution structure determination. The form II crystals have the unusual property that their maximum resolution of diffraction and resistance to radiation damage are enhanced by either crystallization in the presence of or soaking with double-stranded DNA primer-template mimics. These crystals may permit structural studies of catalytically relevant complexes and eventually enable us to experimentally observe successive steps in the reverse transcription process.
引用
收藏
页码:10895 / 10899
页数:5
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